- EMDB-5721: Structure of the flexible N-terminal region of Yersinia enterocol... -
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Basic information
Entry
Database: EMDB / ID: EMD-5721
Title
Structure of the flexible N-terminal region of Yersinia enterocolitica secretin YscC
Map data
Reconstruction of N-terminal region of YscC
Sample
Sample: YscC secretin from Yersinia enterocolitica
Protein or peptide: YscC secretin
Keywords
type III secretion system / Yersinia enterocolitica / Gram-negative bacteria / YscC / secretin / cryo-electron microscopy / outer membrane / N-terminal region
Function / homology
Function and homology information
type III protein secretion system complex / type II protein secretion system complex / protein secretion by the type III secretion system / cell outer membrane / identical protein binding Similarity search - Function
: / SPI-1 type 3 secretion system secretin, N0 domain / Type III secretion system outer membrane pore YscC/HrcC / Bacterial type II secretion system protein D signature. / Type II secretion system protein GspD, conserved site / NolW-like / Bacterial type II/III secretion system short domain / NolW-like superfamily / Type II/III secretion system / Bacterial type II and III secretion system protein Similarity search - Domain/homology
Journal: Structure / Year: 2013 Title: Structure of the dodecameric Yersinia enterocolitica secretin YscC and its trypsin-resistant core. Authors: Julia Kowal / Mohamed Chami / Philippe Ringler / Shirley A Müller / Mikhail Kudryashev / Daniel Castaño-Díez / Marlise Amstutz / Guy R Cornelis / Henning Stahlberg / Andreas Engel / Abstract: The type III secretion system machinery, also known as the injectisome, delivers bacterial effector proteins into eukaryotic cells during infection. The outer membrane YscC secretin is a major part ...The type III secretion system machinery, also known as the injectisome, delivers bacterial effector proteins into eukaryotic cells during infection. The outer membrane YscC secretin is a major part of Yersinia enterocolitica's injectisome and is among the first components to assemble, solely assisted by its pilotin, YscW. We have determined the three-dimensional structures of the native complex and its protease-resistant core to 12 Å resolution by cryo-electron microscopy (cryo-EM) and show that YscC forms a dodecameric complex. Cryo-EM of YscC reconstituted into proteoliposomes defines the secretin's membrane-spanning region. Native YscC consists of an outer membrane ring connected via a thin cylindrical wall to a conical, periplasmic region that exposes N-terminal petals connected by flexible linkers. These petals harbor the binding site of YscD, a component of the inner membrane ring. A change in their orientation adapts the length of the YscC secretin and facilitates its interaction with YscD.
History
Deposition
Jul 16, 2013
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Header (metadata) release
Nov 13, 2013
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Map release
Nov 13, 2013
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Update
Dec 18, 2013
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Current status
Dec 18, 2013
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
pH: 7.8 Details: 10 mM Tris-HCl, 100 mM NaCl, 0.1 mM EDTA, 0.04% DDM
Grid
Details: 200 mesh Cu grid, covered with a very thin additional continuous carbon film, glow-discharged
Vitrification
Cryogen name: ETHANE / Chamber humidity: 95 % / Instrument: FEI VITROBOT MARK IV / Method: Plunging immediately after blotting.
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Electron microscopy
Microscope
FEI/PHILIPS CM200FEG
Date
Oct 1, 2010
Image recording
Category: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: PRIMESCAN / Digitization - Sampling interval: 5 µm / Number real images: 100 / Average electron dose: 20 e/Å2
Electron beam
Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
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