{"entity": "publication", "iuid": "d5c5d050cafe450abca11b51608c0a52", "timestamp": "2026-03-16T17:58:55.999Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/d5c5d050cafe450abca11b51608c0a52.json"}, "display": {"href": "https://publications.scilifelab.se/publication/d5c5d050cafe450abca11b51608c0a52"}}, "title": "RipD (Rv1566c) from Mycobacterium tuberculosis: adaptation of an NlpC/p60 domain to a non-catalytic peptidoglycan-binding function.", "authors": [{"family": "B\u00f6th", "given": "Dominic", "initials": "D"}, {"family": "Steiner", "given": "Eva Maria", "initials": "EM"}, {"family": "Izumi", "given": "Atsushi", "initials": "A"}, {"family": "Schneider", "given": "Gunter", "initials": "G"}, {"family": "Schnell", "given": "Robert", "initials": "R"}], "type": "journal article", "published": "2014-01-01", "journal": {"volume": "457", "issn": "1470-8728", "issue": "1", "pages": "33-41", "title": "Biochem. J.", "issn-l": "0264-6021"}, "abstract": "Enzymes carrying NlpC/p60 domains, for instance RipA and RipB from Mycobacterium tuberculosis, are bacterial peptidoglycan hydrolases that cleave the peptide stems and contribute to cell wall remodelling during cell division. A member of this protein family, RipD (Rv1566c) from M. tuberculosis described in the present study, displays sequence alterations in the NlpC/p60 catalytic triad and carries a pentapeptide repeat at its C-terminus. Bioinformatics analysis revealed RipD-like proteins in eleven mycobacterial genomes, whereas similar pentapeptide repeats occur in cell-wall-localized bacterial proteins and in a mycobacteriophage. In contrast with previously known members of the NlpC/p60 family, RipD does not show peptidoglycan hydrolase activity, which is consistent with the sequence alterations at the catalytic site. A strong interaction of the catalytically inactive core domain with peptidoglycan is however retained, presenting the first example of the NlpC/p60 domains that evolved to a non-catalytic peptidoglycan-binding function. Full-length RipD carrying the C-terminal repeat shows, however, a decrease in binding affinity to peptidoglycan, suggesting that the C-terminal tail modulates the interaction with bacterial cell wall components. The pentapeptide repeat at the C-terminus does not adopt a defined secondary structure in solution which is in accordance with results from the 1.17 \u00c5 (1 \u00c5=0.1 nm) crystal structure of the protein carrying two repeat units.", "doi": "10.1042/BJ20131227", "pmid": "24107184", "labels": {"Protein Science Facility (PSF)": null}, "xrefs": [{"db": "pii", "key": "BJ20131227"}], "notes": [], "created": "2017-05-04T15:03:51.793Z", "modified": "2017-09-06T11:42:09.387Z"}