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14–17 Mar 2022
Europe/Berlin timezone

Direct interaction of a chaperone-bound type three secretion substrate with the export gate

16 Mar 2022, 09:20
20m
Talk Biologic Structure, Function, Reactivity, and Regulation Biocrystallography: Signalling and Macromolecular Complexes

Speaker

Dominic Gilzer

Description

Type III secretion systems (T3SS) are bacterial molecular assemblies employed to inject effector proteins in host cells. We present the structure of a T3S export gate with a substrate:chaperone complex. Following a divide-and-conquer strategy, we first determined the structure of the previously uncharacterized substrate:chaperone complex at higher resolution. Our ternary complex marks the first instance where the substrate directly binds to the export gate instead of mediation by the chaperone.

Primary author

Dominic Gilzer

Co-authors

Madeleine Schreiner Prof. Hartmut Niemann

Presentation materials