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6F2D

A FliPQR complex forms the core of the Salmonella type III secretion system export apparatus.

Summary for 6F2D
Entry DOI10.2210/pdb6f2d/pdb
EMDB information4173
DescriptorFlagellar biosynthetic protein FliP, Flagellar biosynthetic protein FliR, Flagellar biosynthetic protein FliQ (3 entities in total)
Functional Keywordst3ss, flagella, cryo-em, export, membrane protein, protein transport
Biological sourceSalmonella enterica subsp. enterica
More
Total number of polymer chains10
Total formula weight205341.32
Authors
Johnson, S.,Kuhlen, L.,Abrusci, P.,Lea, S.M. (deposition date: 2017-11-24, release date: 2018-07-04, Last modification date: 2024-05-15)
Primary citationKuhlen, L.,Abrusci, P.,Johnson, S.,Gault, J.,Deme, J.,Caesar, J.,Dietsche, T.,Mebrhatu, M.T.,Ganief, T.,Macek, B.,Wagner, S.,Robinson, C.V.,Lea, S.M.
Structure of the core of the type III secretion system export apparatus.
Nat. Struct. Mol. Biol., 25:583-590, 2018
Cited by
PubMed Abstract: Export of proteins through type III secretion systems is critical for motility and virulence of many major bacterial pathogens. Three putative integral membrane proteins (FliP, FliQ, FliR) are suggested to form the core of an export gate in the inner membrane, but their structure, assembly and location within the final nanomachine remain unclear. Here, we present the cryoelectron microscopy structure of the Salmonella Typhimurium FliP-FliQ-FliR complex at 4.2 Å. None of the subunits adopt canonical integral membrane protein topologies, and common helix-turn-helix structural elements allow them to form a helical assembly with 5:4:1 stoichiometry. Fitting of the structure into reconstructions of intact secretion systems, combined with cross-linking, localize the export gate as a core component of the periplasmic portion of the machinery. This study thereby identifies the export gate as a key element of the secretion channel and implies that it primes the helical architecture of the components assembling downstream.
PubMed: 29967543
DOI: 10.1038/s41594-018-0086-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.2 Å)
Structure validation

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数据于2025-06-18公开中

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