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

Protein Science : a Publication of the Protein Society
Ivonne BernalMichael Kolbe

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 oligomerization domain (InvCΔ79) and map the amino acids suggested for ATPase intersubunit interaction, binding to other T3SS proteins and chaperone-effector recognition. Furthermore, we validate the InvC ATP-binding site by co-crystallization of InvCΔ79 with ATPγS (2.65 å) and ADP (2.80 å). Upon ATP-analogue recognition, these structures reveal remodeling of the ATP-binding site and conformational changes of two loops located outside of the catalytic site....Continue Reading

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Citations

Mar 17, 2021·Proceedings of the National Academy of Sciences of the United States of America·Marc-André LeBlancMarcelo C Sousa

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Methods Mentioned

BETA
light scattering
circular dichroism
electrophoresis

Software Mentioned

OPUS
Coot
Mass Lynx
ASTRA
Phaser
Pymol
refine
PHENIX

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