- EMDB-11780: Apo-state type 3 secretion system export apparatus complex from S... -
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基本情報
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データベース: EMDB / ID: EMD-11780
タイトル
Apo-state type 3 secretion system export apparatus complex from Salmonella enterica typhimurium
マップデータ
Postprocess Bfactor: -30
試料
複合体: Export apparatus core complex with inner rod and needle filament proteins PrgJ and PrgI.
タンパク質・ペプチド: Surface presentation of antigens protein SpaP
タンパク質・ペプチド: Surface presentation of antigens protein SpaR
タンパク質・ペプチド: Surface presentation of antigens protein SpaQ
タンパク質・ペプチド: Protein PrgJ
タンパク質・ペプチド: Protein PrgI
キーワード
T3SS / Export Apparatus / Injectisome / Needle Complex / PROTEIN TRANSPORT
機能・相同性
機能・相同性情報
The IPAF inflammasome / type III protein secretion system complex / protein secretion by the type III secretion system / bacterial-type flagellum-dependent swarming motility / bacterial-type flagellum assembly / protein secretion / protein targeting / protein transport / cell surface / extracellular region ...The IPAF inflammasome / type III protein secretion system complex / protein secretion by the type III secretion system / bacterial-type flagellum-dependent swarming motility / bacterial-type flagellum assembly / protein secretion / protein targeting / protein transport / cell surface / extracellular region / identical protein binding / plasma membrane 類似検索 - 分子機能
: / Type III secretion protein SpaR/YscT / Type III secretion protein HrpO / Yop virulence translocation protein R / Type III secretion, needle-protein-like / Type III secretion, needle-protein-like superfamily / Type III secretion needle MxiH, YscF, SsaG, EprI, PscF, EscF / Type III secretion system, needle protein / Type III secretion system inner membrane R protein / Bacterial export protein family 3 ...: / Type III secretion protein SpaR/YscT / Type III secretion protein HrpO / Yop virulence translocation protein R / Type III secretion, needle-protein-like / Type III secretion, needle-protein-like superfamily / Type III secretion needle MxiH, YscF, SsaG, EprI, PscF, EscF / Type III secretion system, needle protein / Type III secretion system inner membrane R protein / Bacterial export protein family 3 / Bacterial export proteins, family 1 / Bacterial export proteins, family 3 / Flagella transport protein fliP family signature 1. / Type III secretion system inner membrane P protein / FliP family / Flagella transport protein fliP family signature 2. 類似検索 - ドメイン・相同性
Surface presentation of antigens protein SpaQ / Surface presentation of antigens protein SpaP / Surface presentation of antigens protein SpaR / SPI-1 type 3 secretion system needle filament protein / Protein PrgJ 類似検索 - 構成要素
ジャーナル: Nat Commun / 年: 2021 タイトル: Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation. 著者: Sean Miletic / Dirk Fahrenkamp / Nikolaus Goessweiner-Mohr / Jiri Wald / Maurice Pantel / Oliver Vesper / Vadim Kotov / Thomas C Marlovits / 要旨: Many bacterial pathogens rely on virulent type III secretion systems (T3SSs) or injectisomes to translocate effector proteins in order to establish infection. The central component of the injectisome ...Many bacterial pathogens rely on virulent type III secretion systems (T3SSs) or injectisomes to translocate effector proteins in order to establish infection. The central component of the injectisome is the needle complex which assembles a continuous conduit crossing the bacterial envelope and the host cell membrane to mediate effector protein translocation. However, the molecular principles underlying type III secretion remain elusive. Here, we report a structure of an active Salmonella enterica serovar Typhimurium needle complex engaged with the effector protein SptP in two functional states, revealing the complete 800Å-long secretion conduit and unraveling the critical role of the export apparatus (EA) subcomplex in type III secretion. Unfolded substrates enter the EA through a hydrophilic constriction formed by SpaQ proteins, which enables side chain-independent substrate transport. Above, a methionine gasket formed by SpaP proteins functions as a gate that dilates to accommodate substrates while preventing leaky pore formation. Following gate penetration, a moveable SpaR loop first folds up to then support substrate transport. Together, these findings establish the molecular basis for substrate translocation through T3SSs and improve our understanding of bacterial pathogenicity and motility.