2KHP

Solution structure of Glutaredoxin from Brucella melitensis


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Comparative analysis of glutaredoxin domains from bacterial opportunistic pathogens.

Leeper, T.Zhang, S.Van Voorhis, W.C.Myler, P.J.Varani, G.

(2011) Acta Crystallogr Sect F Struct Biol Cryst Commun 67: 1141-1147

  • DOI: https://doi.org/10.1107/S1744309111012346
  • Primary Citation of Related Structures:  
    2KHP, 2KLX

  • PubMed Abstract: 

    Glutaredoxin proteins (GLXRs) are essential components of the glutathione system that reductively detoxify substances such as arsenic and peroxides and are important in the synthesis of DNA via ribonucleotide reductases. NMR solution structures of glutaredoxin domains from two Gram-negative opportunistic pathogens, Brucella melitensis and Bartonella henselae, are presented. These domains lack the N-terminal helix that is frequently present in eukaryotic GLXRs. The conserved active-site cysteines adopt canonical proline/tyrosine-stabilized geometries. A difference in the angle of α-helix 2 relative to the β-sheet surface and the presence of an extended loop in the human sequence suggests potential regulatory regions and/or protein-protein interaction motifs. This observation is consistent with mutations in this region that suppress defects in GLXR-ribonucleotide reductase interactions. These differences between the human and bacterial forms are adjacent to the dithiol active site and may permit species-selective drug design.


  • Organizational Affiliation

    School of Medicine, University of Washington, Seattle, WA 98195, USA. tleeper@uakron.edu


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GLUTAREDOXIN92Brucella melitensisMutation(s): 0 
Gene Names: BMEI0184
UniProt
Find proteins for Q8YJA2 (Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094))
Explore Q8YJA2 
Go to UniProtKB:  Q8YJA2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8YJA2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-05-05
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2011-10-05
    Changes: Database references
  • Version 1.3: 2020-02-26
    Changes: Data collection, Database references, Other