{"entity": "researcher", "timestamp": "2026-06-09T02:36:18.404Z", "family": "Sauer-Eriksson", "given": "A Elisabeth", "initials": "AE", "orcid": "0000-0003-0124-0199", "affiliations": ["Department of Chemistry, Ume\u00e5 University, SE-901 87 Ume\u00e5, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95"}}, "publications": [{"entity": "publication", "iuid": "17cc8dd239614f7a9b676fd4294a07ba", "links": {"self": {"href": "https://publications.scilifelab.se/publication/17cc8dd239614f7a9b676fd4294a07ba.json"}, "display": {"href": "https://publications.scilifelab.se/publication/17cc8dd239614f7a9b676fd4294a07ba"}}, "title": "Exploring Helical Fraying Linked to Dynamics and Catalysis in Adenylate Kinase.", "authors": [{"family": "Mattsson", "given": "Jonna", "initials": "J"}, {"family": "Phoeurk", "given": "Chanrith", "initials": "C"}, {"family": "Schierholz", "given": "L\u00e9on", "initials": "L"}, {"family": "Mushtaq", "given": "Ameeq Ul", "initials": "AU"}, {"family": "Rodriguez Buitrago", "given": "Jhon Alexander", "initials": "JA"}, {"family": "Rogne", "given": "Per", "initials": "P", "orcid": "0000-0002-3687-9200", "researcher": {"href": "https://publications.scilifelab.se/researcher/31042ecc88a94cd6b97cef0508da93fd.json"}}, {"family": "Sauer-Eriksson", "given": "A Elisabeth", "initials": "AE", "orcid": "0000-0003-0124-0199", "researcher": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}}, {"family": "Wolf-Watz", "given": "Magnus", "initials": "M", "orcid": "0000-0002-9098-7974", "researcher": {"href": "https://publications.scilifelab.se/researcher/8c6ea8f5c456428db21b1085ad541538.json"}}], "type": "journal article", "published": "2025-10-21", "journal": {"title": "Biochemistry", "issn": "1520-4995", "volume": "64", "issue": "20", "pages": "4281-4295", "issn-l": "0006-2960"}, "abstract": "Conformational dynamics is a fundamental aspect of enzymatic catalysis that, for example, can be linked to ligand binding and release, assembly of the active site, and the catalytic mechanism. The essential and metabolic enzyme adenylate kinase (AK) undergoes large-scale conformational changes in response to binding of its substrates ATP and AMP. As such, it has been intensely studied in search of linkages between dynamics and catalysis. For a complex conformational change to occur in a protein, whether it is of an induced fit or conformational selection nature, changes at several hinges are often required. Here, based on a comparative structure-function analysis of AK enzymes from E. coli and the archaea Odinarchaeota and from human AK1, we found that conformational changes in the enzymes are to a varying degree linked to bending, fraying, or unfolding/folding events of the termini of \u03b1-helices observed in various structural hot spots of the enzymes. The findings contribute with a mechanistic angle to how enzymatic dynamics and catalysis relate to the plasticity of the termini of \u03b1-helices.", "doi": "10.1021/acs.biochem.5c00306", "pmid": "41042980", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC12548092"}], "notes": [], "created": "2025-11-25T19:26:48.320Z", "modified": "2025-11-25T19:26:48.339Z"}, {"entity": "publication", "iuid": "e45d50497d0a46859df9cff25bf95fda", "links": {"self": {"href": "https://publications.scilifelab.se/publication/e45d50497d0a46859df9cff25bf95fda.json"}, "display": {"href": "https://publications.scilifelab.se/publication/e45d50497d0a46859df9cff25bf95fda"}}, "title": "Magnesium induced structural reorganization in the active site of adenylate kinase.", "authors": [{"family": "Nam", "given": "Kwangho", "initials": "K", "orcid": "0000-0003-0723-7839", "researcher": {"href": "https://publications.scilifelab.se/researcher/29b33d801f244b6aac48a9d626962770.json"}}, {"family": "Thodika", "given": "Abdul Raafik Arattu", "initials": "ARA", "orcid": "0009-0001-4973-5265", "researcher": {"href": "https://publications.scilifelab.se/researcher/e85cd5c166044d3fb45c07ca33ebc2e9.json"}}, {"family": "Tischlik", "given": "Sonja", "initials": "S", "orcid": "0000-0001-7518-2441", "researcher": {"href": "https://publications.scilifelab.se/researcher/d2677763e4c64cca828e8ae78a1b4645.json"}}, {"family": "Phoeurk", "given": "Chanrith", "initials": "C", "orcid": "0000-0002-8025-4232", "researcher": {"href": "https://publications.scilifelab.se/researcher/ec49e730932846aa96826a5fffbab6c5.json"}}, {"family": "Nagy", "given": "Tam\u00e1s Mil\u00e1n", "initials": "TM", "orcid": "0000-0003-4766-1992", "researcher": {"href": "https://publications.scilifelab.se/researcher/22a9fd6e6a4e46b2ae2bc0166f62e092.json"}}, {"family": "Schierholz", "given": "L\u00e9on", "initials": "L"}, {"family": "\u00c5d\u00e9n", "given": "J\u00f6rgen", "initials": "J", "orcid": "0000-0002-4480-1219", "researcher": {"href": "https://publications.scilifelab.se/researcher/00206abad0de45eb90dc6bd3d5f3cf22.json"}}, {"family": "Rogne", "given": "Per", "initials": "P", "orcid": "0000-0002-3687-9200", "researcher": {"href": "https://publications.scilifelab.se/researcher/31042ecc88a94cd6b97cef0508da93fd.json"}}, {"family": "Drescher", "given": "Malte", "initials": "M", "orcid": "0000-0002-3571-3452", "researcher": {"href": "https://publications.scilifelab.se/researcher/35108424964e43fbba3e749d8eca0b5b.json"}}, {"family": "Sauer-Eriksson", "given": "A Elisabeth", "initials": "AE", "orcid": "0000-0003-0124-0199", "researcher": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}}, {"family": "Wolf-Watz", "given": "Magnus", "initials": "M", "orcid": "0000-0002-9098-7974", "researcher": {"href": "https://publications.scilifelab.se/researcher/8c6ea8f5c456428db21b1085ad541538.json"}}], "type": "journal article", "published": "2024-08-09", "journal": {"title": "Sci Adv", "issn": "2375-2548", "volume": "10", "issue": "32", "pages": "eado5504", "issn-l": "2375-2548"}, "abstract": "Phosphoryl transfer is a fundamental reaction in cellular signaling and metabolism that requires Mg2+ as an essential cofactor. While the primary function of Mg2+ is electrostatic activation of substrates, such as ATP, the full spectrum of catalytic mechanisms exerted by Mg2+ is not known. In this study, we integrate structural biology methods, molecular dynamic (MD) simulations, phylogeny, and enzymology assays to provide molecular insights into Mg2+-dependent structural reorganization in the active site of the metabolic enzyme adenylate kinase. Our results demonstrate that Mg2+ induces a conformational rearrangement of the substrates (ATP and ADP), resulting in a 30\u00b0 adjustment of the angle essential for reversible phosphoryl transfer, thereby optimizing it for catalysis. MD simulations revealed transitions between conformational substates that link the fluctuation of the angle to large-scale enzyme dynamics. The findings contribute detailed insight into Mg2+ activation of enzymes and may be relevant for reversible and irreversible phosphoryl transfer reactions.", "doi": "10.1126/sciadv.ado5504", "pmid": "39121211", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC11313852"}], "notes": [], "created": "2024-11-13T19:36:50.332Z", "modified": "2025-10-17T13:03:52.837Z"}, {"entity": "publication", "iuid": "53956265bf60408f8bef4f64b6bb2e60", "links": {"self": {"href": "https://publications.scilifelab.se/publication/53956265bf60408f8bef4f64b6bb2e60.json"}, "display": {"href": "https://publications.scilifelab.se/publication/53956265bf60408f8bef4f64b6bb2e60"}}, "title": "Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate by E. coli Adenylate Kinase.", "authors": [{"family": "Tischlik", "given": "Sonja", "initials": "S"}, {"family": "Oelker", "given": "Melanie", "initials": "M"}, {"family": "Rogne", "given": "Per", "initials": "P", "orcid": "0000-0002-3687-9200", "researcher": {"href": "https://publications.scilifelab.se/researcher/31042ecc88a94cd6b97cef0508da93fd.json"}}, {"family": "Sauer-Eriksson", "given": "A Elisabeth", "initials": "AE", "orcid": "0000-0003-0124-0199", "researcher": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}}, {"family": "Drescher", "given": "Malte", "initials": "M", "orcid": "0000-0002-3571-3452", "researcher": {"href": "https://publications.scilifelab.se/researcher/35108424964e43fbba3e749d8eca0b5b.json"}}, {"family": "Wolf-Watz", "given": "Magnus", "initials": "M", "orcid": "0000-0002-9098-7974", "researcher": {"href": "https://publications.scilifelab.se/researcher/8c6ea8f5c456428db21b1085ad541538.json"}}], "type": "journal article", "published": "2023-08-01", "journal": {"title": "Biochemistry", "issn": "1520-4995", "volume": "62", "issue": "15", "pages": "2238-2243", "issn-l": "0006-2960"}, "abstract": "Adenylate kinases play a crucial role in cellular energy homeostasis through the interconversion of ATP, AMP, and ADP in all living organisms. Here, we explore how adenylate kinase (AdK) from Escherichia coli interacts with diadenosine tetraphosphate (AP4A), a putative alarmone associated with transcriptional regulation, stress, and DNA damage response. From a combination of EPR and NMR spectroscopy together with X-ray crystallography, we found that AdK interacts with AP4A with two distinct modes that occur on disparate time scales. First, AdK dynamically interconverts between open and closed states with equal weights in the presence of AP4A. On a much slower time scale, AdK hydrolyses AP4A, and we suggest that the dynamically accessed substrate-bound open AdK conformation enables this hydrolytic activity. The partitioning of the enzyme into open and closed states is discussed in relation to a recently proposed linkage between active site dynamics and collective conformational dynamics.", "doi": "10.1021/acs.biochem.3c00189", "pmid": "37418448", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC10399197"}], "notes": [], "created": "2023-12-01T21:38:02.891Z", "modified": "2025-10-17T13:03:53.617Z"}, {"entity": "publication", "iuid": "0fa6a6d0d98e4cdc824c41a447297873", "links": {"self": {"href": "https://publications.scilifelab.se/publication/0fa6a6d0d98e4cdc824c41a447297873.json"}, "display": {"href": "https://publications.scilifelab.se/publication/0fa6a6d0d98e4cdc824c41a447297873"}}, "title": "Insights into the evolution of enzymatic specificity and catalysis: From Asgard archaea to human adenylate kinases.", "authors": [{"family": "Verma", "given": "Apoorv", "initials": "A", "orcid": "0000-0002-8726-0870", "researcher": {"href": "https://publications.scilifelab.se/researcher/570887d2afe6478da2130ad606cf94e9.json"}}, {"family": "\u00c5berg-Zingmark", "given": "Emma", "initials": "E", "orcid": "0000-0002-5052-5214", "researcher": {"href": "https://publications.scilifelab.se/researcher/82284b92733343d7ba9c03be8bc85fca.json"}}, {"family": "Sparrman", "given": "Tobias", "initials": "T", "orcid": "0000-0002-4442-6367", "researcher": {"href": "https://publications.scilifelab.se/researcher/f0d27dbd2f014795b1f7aa164d34bada.json"}}, {"family": "Mushtaq", "given": "Ameeq Ul", "initials": "AU", "orcid": "0000-0002-5636-2567", "researcher": {"href": "https://publications.scilifelab.se/researcher/d8b77280f8a9463a9af768275bc80ae9.json"}}, {"family": "Rogne", "given": "Per", "initials": "P", "orcid": "0000-0002-3687-9200", "researcher": {"href": "https://publications.scilifelab.se/researcher/31042ecc88a94cd6b97cef0508da93fd.json"}}, {"family": "Grundstr\u00f6m", "given": "Christin", "initials": "C"}, {"family": "Berntsson", "given": "Ronnie", "initials": "R", "orcid": "0000-0001-6848-322X", "researcher": {"href": "https://publications.scilifelab.se/researcher/e78d8a69e46241bc8a79ede3df38ebdf.json"}}, {"family": "Sauer", "given": "Uwe H", "initials": "UH", "orcid": "0000-0002-3420-439X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5d011e944ae54d47aed374d548007812.json"}}, {"family": "Backman", "given": "Lars", "initials": "L", "orcid": "0000-0003-3044-1256", "researcher": {"href": "https://publications.scilifelab.se/researcher/99a60ee46b814b5a822c9c93e46ffe42.json"}}, {"family": "Nam", "given": "Kwangho", "initials": "K", "orcid": "0000-0003-0723-7839", "researcher": {"href": "https://publications.scilifelab.se/researcher/29b33d801f244b6aac48a9d626962770.json"}}, {"family": "Sauer-Eriksson", "given": "Elisabeth", "initials": "E", "orcid": "0000-0003-0124-0199", "researcher": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}}, {"family": "Wolf-Watz", "given": "Magnus", "initials": "M", "orcid": "0000-0002-9098-7974", "researcher": {"href": "https://publications.scilifelab.se/researcher/8c6ea8f5c456428db21b1085ad541538.json"}}], "type": "journal article", "published": "2022-11-04", "journal": {"title": "Sci Adv", "issn": "2375-2548", "volume": "8", "issue": "44", "pages": "eabm4089", "issn-l": "2375-2548"}, "abstract": "Enzymatic catalysis is critically dependent on selectivity, active site architecture, and dynamics. To contribute insights into the interplay of these properties, we established an approach with NMR, crystallography, and MD simulations focused on the ubiquitous phosphotransferase adenylate kinase (AK) isolated from <i>Odinarchaeota<\/i> (OdinAK). <i>Odinarchaeota<\/i> belongs to the Asgard archaeal phylum that is believed to be the closest known ancestor to eukaryotes. We show that OdinAK is a hyperthermophilic trimer that, contrary to other AK family members, can use all NTPs for its phosphorylation reaction. Crystallographic structures of OdinAK-NTP complexes revealed a universal NTP-binding motif, while <sup>19<\/sup>F NMR experiments uncovered a conserved and rate-limiting dynamic signature. As a consequence of trimerization, the active site of OdinAK was found to be lacking a critical catalytic residue and is therefore considered to be \"atypical.\" On the basis of discovered relationships with human monomeric homologs, our findings are discussed in terms of evolution of enzymatic substrate specificity and cold adaptation.", "doi": "10.1126/sciadv.abm4089", "pmid": "36332013", "labels": {"Swedish NMR Centre": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC9635829"}], "notes": [], "created": "2022-11-28T13:05:26.193Z", "modified": "2025-10-17T13:03:54.457Z"}, {"entity": "publication", "iuid": "0acc2048f2074e63bddc5c1c8e0bc768", "links": {"self": {"href": "https://publications.scilifelab.se/publication/0acc2048f2074e63bddc5c1c8e0bc768.json"}, "display": {"href": "https://publications.scilifelab.se/publication/0acc2048f2074e63bddc5c1c8e0bc768"}}, "title": "Structural basis for transthyretin amyloid formation in vitreous body of the eye.", "authors": [{"family": "Iakovleva", "given": "Irina", "initials": "I", "orcid": "0000-0002-9500-5917", "researcher": {"href": "https://publications.scilifelab.se/researcher/b5fd05e56e164227b137bac9a879af58.json"}}, {"family": "Hall", "given": "Michael", "initials": "M", "orcid": "0000-0003-0864-9798", "researcher": {"href": "https://publications.scilifelab.se/researcher/7489a92a241f4d0d9f8ef6eb4fcb3858.json"}}, {"family": "Oelker", "given": "Melanie", "initials": "M", "orcid": "0000-0001-7301-8445", "researcher": {"href": "https://publications.scilifelab.se/researcher/0d4b43ce3822421e998c7ecead0f2e1a.json"}}, {"family": "Sandblad", "given": "Linda", "initials": "L", "orcid": "0000-0003-3492-3287", "researcher": {"href": "https://publications.scilifelab.se/researcher/070825e0190a4e9a932e79663d2bc89f.json"}}, {"family": "Anan", "given": "Intissar", "initials": "I", "orcid": "0000-0003-2874-7643", "researcher": {"href": "https://publications.scilifelab.se/researcher/923515859dae4f16ae6f4cee53515f98.json"}}, {"family": "Sauer-Eriksson", "given": "A Elisabeth", "initials": "AE", "orcid": "0000-0003-0124-0199", "researcher": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}}], "type": "journal article", "published": "2021-12-08", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "12", "issue": "1", "pages": "7141", "issn-l": "2041-1723"}, "abstract": "Amyloid transthyretin (ATTR) amyloidosis is characterized by the abnormal accumulation of ATTR fibrils in multiple organs. However, the structure of ATTR fibrils from the eye is poorly understood. Here, we used cryo-EM to structurally characterize vitreous body ATTR fibrils. These structures were distinct from previously characterized heart fibrils, even though both have the same mutation and type A pathology. Differences were observed at several structural levels: in both the number and arrangement of protofilaments, and the conformation of the protein fibril in each layer of protofilaments. Thus, our results show that ATTR protein structure and its assembly into protofilaments in the type A fibrils can vary between patients carrying the same mutation. By analyzing and matching the interfaces between the amino acids in the ATTR fibril with those in the natively folded TTR, we are able to propose a mechanism for the structural conversion of TTR into a fibrillar form.", "doi": "10.1038/s41467-021-27481-4", "pmid": "34880242", "labels": {"Cryo-EM": "Collaborative", "Structural Proteomics": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41467-021-27481-4"}, {"db": "pmc", "key": "PMC8654999"}], "notes": [], "created": "2021-12-09T13:57:20.280Z", "modified": "2022-01-03T10:03:27.020Z"}, {"entity": "publication", "iuid": "81e7c7a8721c401db24730496b0fb38d", "links": {"self": {"href": "https://publications.scilifelab.se/publication/81e7c7a8721c401db24730496b0fb38d.json"}, "display": {"href": "https://publications.scilifelab.se/publication/81e7c7a8721c401db24730496b0fb38d"}}, "title": "Structural Basis for GTP versus ATP Selectivity in the NMP Kinase AK3.", "authors": [{"family": "Rogne", "given": "Per", "initials": "P"}, {"family": "Dulko-Smith", "given": "Beata", "initials": "B"}, {"family": "Goodman", "given": "Jack", "initials": "J"}, {"family": "Rosselin", "given": "Marie", "initials": "M"}, {"family": "Grundstr\u00f6m", "given": "Christin", "initials": "C"}, {"family": "Hedberg", "given": "Christian", "initials": "C"}, {"family": "Nam", "given": "Kwangho", "initials": "K", "orcid": "0000-0003-0723-7839", "researcher": {"href": "https://publications.scilifelab.se/researcher/29b33d801f244b6aac48a9d626962770.json"}}, {"family": "Sauer-Eriksson", "given": "A Elisabeth", "initials": "AE", "orcid": "0000-0003-0124-0199", "researcher": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}}, {"family": "Wolf-Watz", "given": "Magnus", "initials": "M", "orcid": "0000-0002-9098-7974", "researcher": {"href": "https://publications.scilifelab.se/researcher/8c6ea8f5c456428db21b1085ad541538.json"}}], "type": "journal article", "published": "2020-09-29", "journal": {"title": "Biochemistry", "issn": "1520-4995", "volume": "59", "issue": "38", "pages": "3570-3581", "issn-l": "0006-2960"}, "abstract": "ATP and GTP are exceptionally important molecules in biology with multiple, and often discrete, functions. Therefore, enzymes that bind to either of them must develop robust mechanisms to selectively utilize one or the other. Here, this specific problem is addressed by molecular studies of the human NMP kinase AK3, which uses GTP to phosphorylate AMP. AK3 plays an important role in the citric acid cycle, where it is responsible for GTP/GDP recycling. By combining a structural biology approach with functional experiments, we present a comprehensive structural and mechanistic understanding of the enzyme. We discovered that AK3 functions by recruitment of GTP to the active site, while ATP is rejected and nonproductively bound to the AMP binding site. Consequently, ATP acts as an inhibitor with respect to GTP and AMP. The overall features with specific recognition of the correct substrate and nonproductive binding by the incorrect substrate bear a strong similarity to previous findings for the ATP specific NMP kinase adenylate kinase. Taken together, we are now able to provide the fundamental principles for GTP and ATP selectivity in the large NMP kinase family. As a side-result originating from nonlinearity of chemical shifts in GTP and ATP titrations, we find that protein surfaces offer a general and weak binding affinity for both GTP and ATP. These nonspecific interactions likely act to lower the available intracellular GTP and ATP concentrations and may have driven evolution of the Michaelis constants of NMP kinases accordingly.", "doi": "10.1021/acs.biochem.0c00549", "pmid": "32822537", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC8325564"}, {"db": "mid", "key": "NIHMS1725248"}], "notes": [], "created": "2020-11-24T20:29:24.742Z", "modified": "2025-10-17T13:03:56.627Z"}, {"entity": "publication", "iuid": "4dbd4a90582d4043977063a125f3ace5", "links": {"self": {"href": "https://publications.scilifelab.se/publication/4dbd4a90582d4043977063a125f3ace5.json"}, "display": {"href": "https://publications.scilifelab.se/publication/4dbd4a90582d4043977063a125f3ace5"}}, "title": "Nucleation of an Activating Conformational Change by a Cation-\u03c0 Interaction.", "authors": [{"family": "Rogne", "given": "Per", "initials": "P"}, {"family": "Andersson", "given": "David", "initials": "D", "orcid": "0000-0001-8198-1688", "researcher": {"href": "https://publications.scilifelab.se/researcher/193c9aad4bf14efa9163d63ee9310715.json"}}, {"family": "Grundstr\u00f6m", "given": "Christin", "initials": "C"}, {"family": "Sauer-Eriksson", "given": "Elisabeth", "initials": "E", "orcid": "0000-0003-0124-0199", "researcher": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}}, {"family": "Linusson", "given": "Anna", "initials": "A"}, {"family": "Wolf-Watz", "given": "Magnus", "initials": "M", "orcid": "0000-0002-9098-7974", "researcher": {"href": "https://publications.scilifelab.se/researcher/8c6ea8f5c456428db21b1085ad541538.json"}}], "type": "journal article", "published": "2019-08-13", "journal": {"title": "Biochemistry", "issn": "1520-4995", "volume": "58", "issue": "32", "pages": "3408-3412", "issn-l": "0006-2960"}, "abstract": "As a key molecule in biology, adenosine triphosphate (ATP) has numerous crucial functions in, for instance, energetics, post-translational modifications, nucleotide biosynthesis, and cofactor metabolism. Here, we have discovered an intricate interplay between the enzyme adenylate kinase and its substrate ATP. The side chain of an arginine residue was found to be an efficient sensor of the aromatic moiety of ATP through the formation of a strong cation-\u03c0 interaction. In addition to recognition, the interaction was found to have dual functionality. First, it nucleates the activating conformational transition of the ATP binding domain and also affects the specificity in the distant AMP binding domain. In light of the functional consequences resulting from the cation-\u03c0 interaction, it is possible that the mode of ATP recognition may be a useful tool in enzyme design.", "doi": "10.1021/acs.biochem.9b00538", "pmid": "31339702", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [], "notes": [], "created": "2020-01-07T11:37:53.465Z", "modified": "2025-10-17T13:03:57.635Z"}]}