2KHP: Solution structure of Glutaredoxin from Brucella melitensis

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 alpha-helix 2 relative to the beta-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.
PDB ID: 2KHPDownload
MMDB ID: 72387
PDB Deposition Date: 2009/4/10
Updated in MMDB: 2011/10
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2KHP: monomeric; determined by author
Molecular Components in 2KHP
Label Count Molecule
Protein (1 molecule)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB