A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat.

ABSTRACT: InlB, a bacterial agonist of the human receptor tyrosine kinase MET, consists of an N-terminal internalin domain, a central B repeat and three C-terminal GW domains. In all previous structures of full-length InlB or an InlB construct lacking the GW domains (InlB₃₉₂), there was no interpretable electron density for the B repeat. Here, three InlB₃₉₂ crystal structures in which the B repeat is resolved are described. These are the first structures to reveal the relative orientation of the internalin domain and the B repeat. A wild-type structure and two structures of the T332E variant together contain five crystallographically independent molecules. Surprisingly, the threonine-to-glutamate substitution in the B repeat substantially improved the crystallization propensity

SUBMITTER: Geerds C 

PROVIDER: S-EPMC8900821 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature