3ZBJ

Fitting results in the I-layer of the subnanometer structure of the bacterial pKM101 type IV secretion system core complex digested with elastase


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 8.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

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This is version 1.2 of the entry. See complete history


Literature

Structure of a Bacterial Type Iv Secretion Core Complex at Subnanometre Resolution.

Rivera-Calzada, A.Fronzes, R.Savva, C.G.Chandran, V.Lian, P.W.Laeremans, T.Pardon, E.Steyaert, J.Remaut, H.Waksman, G.Orlova, E.V.

(2013) EMBO J 32: 1195

  • DOI: https://doi.org/10.1038/emboj.2013.58
  • Primary Citation of Related Structures:  
    2YPW, 3ZBI, 3ZBJ

  • PubMed Abstract: 

    Type IV secretion (T4S) systems are able to transport DNAs and/or proteins through the membranes of bacteria. They form large multiprotein complexes consisting of 12 proteins termed VirB1-11 and VirD4. VirB7, 9 and 10 assemble into a 1.07 MegaDalton membrane-spanning core complex (CC), around which all other components assemble. This complex is made of two parts, the O-layer inserted in the outer membrane and the I-layer inserted in the inner membrane. While the structure of the O-layer has been solved by X-ray crystallography, there is no detailed structural information on the I-layer. Using high-resolution cryo-electron microscopy and molecular modelling combined with biochemical approaches, we determined the I-layer structure and located its various components in the electron density. Our results provide new structural insights on the CC, from which the essential features of T4S system mechanisms can be derived.


  • Organizational Affiliation

    Department of Biological Sciences, Institute of Structural and Molecular Biology, UCL and Birkbeck, London WC1E 7HX, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRAO PROTEIN
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L, M, N
112Escherichia coli BL21Mutation(s): 0 
UniProt
Find proteins for Q46704 (Escherichia coli)
Explore Q46704 
Go to UniProtKB:  Q46704
Entity Groups  
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UniProt GroupQ46704
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 8.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONIMAGIC

Structure Validation

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Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2013-04-03
    Type: Initial release
  • Version 1.1: 2013-05-01
    Changes: Database references
  • Version 1.2: 2017-08-30
    Changes: Data collection, Refinement description