Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system.

Mushtaq AU, Ådén J, Alam A, Sjöstedt A, Gröbner G

Biomol NMR Assign - (-) - [2022-01-05; online 2022-01-05]

The Hsp100 family member ClpB is a protein disaggregase which solubilizes and reactivates stress-induced protein aggregates in cooperation with the DnaK/Hsp70 chaperone system. In the pathogenic bacterium Francisella tularensis, ClpB is involved in type VI secretion system (T6SS) disassembly through depolymerization of the IglA-IglB sheath. This leads to recycling and reassembly of T6SS components and this process is essential for the virulence of the bacterium. Here we report the backbone chemical shift assignments and 15N relaxation-based backbone dynamics of the N-terminal substrate-binding domain of ClpB (1-156).

Swedish NMR Centre (SNC) [Collaborative]

PubMed 34985724

DOI 10.1007/s12104-021-10062-3

Crossref 10.1007/s12104-021-10062-3

pii: 10.1007/s12104-021-10062-3