1BXW

OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.189 

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Literature

Structure of the outer membrane protein A transmembrane domain.

Pautsch, A., Schulz, G.E.

(1998) Nat Struct Biol 5: 1013-1017

  • DOI: https://doi.org/10.1038/2983
  • Primary Citation of Related Structures:  
    1BXW

  • PubMed Abstract: 

    The outer membrane protein A of Escherichia coli (OmpA) is an intensely studied example in the field of membrane protein folding. We have determined the structure of the OmpA transmembrane domain consisting of residues 1-171, by X-ray diffraction analysis, to a resolution of 2.5 A. It consists of a regular, extended eight-stranded beta-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. Surprisingly, the cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of beta-barrels. The structure constitutes a beta-barrel membrane anchor that appears to be the outer membrane equivalent of the single-chain alpha-helix anchor of the inner membrane.

    • Organizational Affiliation: 

    Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Freiburg im Breisgau, Germany.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (OUTER MEMBRANE PROTEIN A)172Escherichia coli BL21(DE3)Mutation(s): 3 
Gene Names: OMPA
Membrane Entity: Yes 
UniProt
Find proteins for P0A910 (Escherichia coli (strain K12))
Explore P0A910 
Go to UniProtKB:  P0A910
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A910
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
C8E
Query on C8E
Download Ideal Coordinates CCD File 
B [auth A](HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE
C16 H34 O5
FEOZZFHAVXYAMB-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.189 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.18α = 90
b = 77.95β = 91.52
c = 50.93γ = 90
Software Package:
Software NamePurpose
SHARPphasing
REFMACrefinement
XDSdata reduction
CCP4data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-10-14
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-11-29
    Changes: Advisory
  • Version 1.4: 2018-03-14
    Changes: Database references
  • Version 1.5: 2023-02-15
    Changes: Advisory, Database references, Derived calculations