- EMDB-20831: Cryo-EM reconstruction shows that the needle complex's inner ring... -
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Basic information
Entry
Database: EMDB / ID: EMD-20831
Title
Cryo-EM reconstruction shows that the needle complex's inner rings from Salmonella assemble with 23-fold symmetry in the absence of the export apparatus.
Map data
Sample
Complex: Complex of PrgH and PrgK, the protein components of the inner rings of Salmonella's needle complex, assembled in the absence of the export apparatus.
National Institutes of Health/National Institute Of Allergy and Infectious Diseases
United States
Citation
Journal: Proc Natl Acad Sci U S A / Year: 2019 Title: High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway. Authors: Carmen Butan / Maria Lara-Tejero / Wenwei Li / Jun Liu / Jorge E Galán / Abstract: Type III protein secretion systems are essential virulence factors for many important pathogenic bacteria. The entire protein secretion machine is composed of several substructures that organize into ...Type III protein secretion systems are essential virulence factors for many important pathogenic bacteria. The entire protein secretion machine is composed of several substructures that organize into a holostructure or injectisome. The core component of the injectisome is the needle complex, which houses the export apparatus that serves as a gate for the passage of the secreted proteins through the bacterial inner membrane. Here, we describe a high-resolution structure of the export apparatus of the type III secretion system in association with the needle complex and the underlying bacterial membrane, both in isolation and in situ. We show the precise location of the core export apparatus components within the injectisome and bacterial envelope and demonstrate that their deployment results in major membrane remodeling and thinning, which may be central for the protein translocation process. We also show that InvA, a critical export apparatus component, forms a multiring cytoplasmic conduit that provides a pathway for the type III secretion substrates to reach the entrance of the export gate. Combined with structure-guided mutagenesis, our studies provide major insight into potential mechanisms of protein translocation and injectisome assembly.
History
Deposition
Oct 15, 2019
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Header (metadata) release
Nov 13, 2019
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Map release
Jul 1, 2020
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Update
Jul 1, 2020
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Current status
Jul 1, 2020
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Download / File: emd_20831.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel size
X=Y=Z: 1.07 Å
Density
Contour Level
By AUTHOR: 0.0098 / Movie #1: 0.0108
Minimum - Maximum
-0.01748075 - 0.040073305
Average (Standard dev.)
0.00037343317 (±0.0028942786)
Symmetry
Space group: 1
Details
EMDB XML:
Map geometry
Axis order
X
Y
Z
Origin
0
0
0
Dimensions
360
360
360
Spacing
360
360
360
Cell
A=B=C: 385.2 Å α=β=γ: 90.0 °
CCP4 map header:
mode
Image stored as Reals
Å/pix. X/Y/Z
1.07
1.07
1.07
M x/y/z
360
360
360
origin x/y/z
0.000
0.000
0.000
length x/y/z
385.200
385.200
385.200
α/β/γ
90.000
90.000
90.000
MAP C/R/S
1
2
3
start NC/NR/NS
0
0
0
NC/NR/NS
360
360
360
D min/max/mean
-0.017
0.040
0.000
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Supplemental data
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Sample components
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Entire : Complex of PrgH and PrgK, the protein components of the inner rin...
Entire
Name: Complex of PrgH and PrgK, the protein components of the inner rings of Salmonella's needle complex, assembled in the absence of the export apparatus.
Components
Complex: Complex of PrgH and PrgK, the protein components of the inner rings of Salmonella's needle complex, assembled in the absence of the export apparatus.
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Supramolecule #1: Complex of PrgH and PrgK, the protein components of the inner rin...
Supramolecule
Name: Complex of PrgH and PrgK, the protein components of the inner rings of Salmonella's needle complex, assembled in the absence of the export apparatus. type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
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