1C5K

THE STRUCTURE OF TOLB, AN ESSENTIAL COMPONENT OF THE TOL-DEPENDENT TRANSLOCATION SYSTEM AND ITS INTERACTIONS WITH THE TRANSLOCATION DOMAIN OF COLICIN E9


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.234 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9.

Carr, S.Penfold, C.N.Bamford, V.James, R.Hemmings, A.M.

(2000) Structure 8: 57-66

  • DOI: https://doi.org/10.1016/s0969-2126(00)00079-4
  • Primary Citation of Related Structures:  
    1C5K

  • PubMed Abstract: 

    E colicin proteins have three functional domains, each of which is implicated in one of the stages of killing Escherichia coli cells: receptor binding, translocation and cytotoxicity. The central (R) domain is responsible for receptor-binding activity whereas the N-terminal (T) domain mediates translocation, the process by which the C-terminal cytotoxic domain is transported from the receptor to the site of its cytotoxicity. The translocation of enzymatic E colicins like colicin E9 is dependent upon TolB but the details of the process are not known.


  • Organizational Affiliation

    Colicin Research Group, School of Biological Sciences, School of Chemical Sciences, University of East Anglia, Norwich, NR4 7TJ, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (TOLB PROTEIN)439Escherichia coliMutation(s): 0 
UniProt
Find proteins for P0A855 (Escherichia coli (strain K12))
Explore P0A855 
Go to UniProtKB:  P0A855
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A855
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
YB
Query on YB

Download Ideal Coordinates CCD File 
B [auth A]YTTERBIUM (III) ION
Yb
AWSFICBXMUKWSK-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.234 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.58α = 90
b = 40.19β = 110.22
c = 77.66γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-12-06
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Derived calculations