Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC.

ABSTRACT: Translocation of virulence effector proteins through the type III secretion system (T3SS) is essential for the virulence of many medically relevant Gram-negative bacteria. The T3SS ATPases are conserved components that specifically recognize chaperone-effector complexes and energize effector secretion through the system. It is thought that functional T3SS ATPases assemble into a cylindrical structure maintained by their N-terminal domains. Using size-exclusion chromatography coupled to multi-angle light scattering and native mass spectrometry, we show that in the absence of the N-terminal oligomerization domain the Salmonella T3SS ATPase InvC can form monomers and dimers in solution. We also present for the first time a 2.05 å resolution crystal structure of InvC lacking the oligomerizatio

SUBMITTER: Bernal I 

PROVIDER: S-EPMC6739812 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature