2HDI

Crystal structure of the Colicin I receptor Cir from E.coli in complex with receptor binding domain of Colicin Ia.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.191 

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This is version 1.4 of the entry. See complete history


Literature

Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import.

Buchanan, S.K.Lukacik, P.Grizot, S.Ghirlando, R.Ali, M.M.Barnard, T.J.Jakes, K.S.Kienker, P.K.Esser, L.

(2007) EMBO J 26: 2594-2604

  • DOI: https://doi.org/10.1038/sj.emboj.7601693
  • Primary Citation of Related Structures:  
    2HDF, 2HDI

  • PubMed Abstract: 

    Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space, where it inserts into the inner membrane and forms a voltage-dependent ion channel. We determined crystal structures of colicin I receptor alone and in complex with the receptor binding domain of colicin Ia. The receptor undergoes large and unusual conformational changes upon colicin binding, opening at the cell surface and positioning the receptor binding domain of colicin Ia directly above it. We modelled the interaction with full-length colicin Ia to show that the channel forming domain is initially positioned 150 A above the cell surface. Functional data using full-length colicin Ia show that colicin I receptor is necessary for cell surface binding, and suggest that the receptor participates in translocation of colicin Ia across the outer membrane.


  • Organizational Affiliation

    Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. skbuchan@helix.nih.gov


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Colicin I receptor639Escherichia coliMutation(s): 4 
Gene Names: cirA
Membrane Entity: Yes 
UniProt
Find proteins for P17315 (Escherichia coli (strain K12))
Explore P17315 
Go to UniProtKB:  P17315
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP17315
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Colicin-Ia113Escherichia coliMutation(s): 0 
Gene Names: cia
Membrane Entity: Yes 
UniProt
Find proteins for P06716 (Escherichia coli)
Explore P06716 
Go to UniProtKB:  P06716
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06716
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.191 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 132.633α = 90
b = 130.494β = 101.22
c = 56.261γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-05-08
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2021-10-20
    Changes: Database references, Derived calculations
  • Version 1.4: 2023-08-30
    Changes: Data collection, Refinement description