1B2V

HEME-BINDING PROTEIN A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.175 
  • R-Value Observed: 0.177 

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This is version 1.4 of the entry. See complete history


Literature

The crystal structure of HasA, a hemophore secreted by Serratia marcescens.

Arnoux, P.Haser, R.Izadi, N.Lecroisey, A.Delepierre, M.Wandersman, C.Czjzek, M.

(1999) Nat Struct Biol 6: 516-520

  • DOI: https://doi.org/10.1038/9281
  • Primary Citation of Related Structures:  
    1B2V

  • PubMed Abstract: 

    Free iron availability is strongly limited in vertebrate hosts, making the iron acquisition by siderophores inappropriate. Pathogenic bacteria have developed various ways to use the host's iron from iron-containing proteins. Serratia marcescens can use the iron from hemoglobin through the secretion of a hemophore called HasA, which takes up the heme from hemoglobin and shuttles it to the receptor HasR, which in turn, releases heme into the bacterium. We report here the first crystal structure of such a hemophore, bound to a heme group at two different pH values and at a resolution of 1.9 A. The structure reveals a new original fold and suggests a hypothetical mechanism for both heme uptake and release.


  • Organizational Affiliation

    Laboratoire d'Architecture et Fonction des Macromolécules Biologiques UPR 9039, Institut de Biologie Structurale et Microbiologie, CNRS, Marseille, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (HEME-BINDING PROTEIN A)188Serratia marcescensMutation(s): 0 
UniProt
Find proteins for Q54450 (Serratia marcescens)
Explore Q54450 
Go to UniProtKB:  Q54450
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ54450
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.175 
  • R-Value Observed: 0.177 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 41.65α = 90
b = 80.66β = 93.58
c = 63.23γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
CCP4data scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-06-24
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2014-11-12
    Changes: Database references, Derived calculations
  • Version 1.4: 2023-12-27
    Changes: Data collection, Database references, Derived calculations