2KHP

Solution structure of Glutaredoxin from Brucella melitensis

Summary for 2KHP

• Entry DOI: 10.2210/pdb2khp/pdb
• NMR Information: BMRB: 16264
• Descriptor: GLUTAREDOXIN (1 entity in total)
• Functional Keywords: glutaredoxin, thioredoxin type domain, ssgcid, electron transport, structural genomics, seattle structural genomics center for infectious disease
• Biological source: Brucella melitensis
• Total number of polymer chains: 1
• Total formula weight: 9956.36

Authors

Zheng, S.,Leeper, T.,Varani, G.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2009-04-10, release date: 2009-05-05, Last modification date: 2020-02-26)

Primary citation

Leeper, T.,Zhang, S.,Van Voorhis, W.C.,Myler, P.J.,Varani, G.
Comparative analysis of glutaredoxin domains from bacterial opportunistic pathogens.
Acta Crystallogr.,Sect.F, 67:1141-1147, 2011

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.

PubMed: 21904064
DOI: 10.1107/S1744309111012346

Experimental method

SOLUTION NMR