Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system

Xing, Qiong; Shi, Ke; Portaliou, Athina; Rossi, Paolo; Economou, Anastassios; Kalodimos, Charalampos G.

doi:10.1038/s41467-018-04137-4

Title: Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system

Journal Article · Wed May 02 00:00:00 EDT 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-04137-4· OSTI ID:1436776

^[1]; Shi, Ke ^[2]; Portaliou, Athina ^[3]; Rossi, Paolo ^[1]; Economou, Anastassios ^[3];

^[1]

St. Jude Children’s Research Hospital, Memphis, TN (United States)
Univ. of Minnesota, Minneapolis, MN (United States)
Katholicke Univ. Leuven (Belgium)

The flagellum and the injectisome enable bacterial locomotion and pathogenesis, respectively. These nanomachines assemble and function using a type III secretion system (T3SS). Exported proteins are delivered to the export apparatus by dedicated cytoplasmic chaperones for their transport through the membrane. The structural and mechanistic basis of this process is poorly understood. Here we report the structures of two ternary complexes among flagellar chaperones (FliT and FliS), protein substrates (the filament-capping FliD and flagellin FliC), and the export gate platform protein FlhA. The substrates do not interact directly with FlhA; however, they are required to induce a binding-competent conformation to the chaperone that exposes the recognition motif featuring a highly conserved sequence recognized by FlhA. The structural data reveal the recognition signal in a class of T3SS proteins and provide new insight into the assembly of key protein complexes at the export gate.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division; US National Inst. of Health; NIH-ORIP HEI

Grant/Contract Number:: AC02-06CH11357; AI094623; NIGMS P41-GM103403; S10 RR029205

OSTI ID:: 1436776

Journal Information:: Nature Communications, Vol. 9, Issue 1; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 48 works

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