1LJU: X-Ray Structure Of C15a Arsenate Reductase From Pi258 Complexed With Arsenite

The mechanism of pI258 arsenate reductase (ArsC) catalyzed arsenate reduction, involving its P-loop structural motif and three redox active cysteines, has been unraveled. All essential intermediates are visualized with x-ray crystallography, and NMR is used to map dynamic regions in a key disulfide intermediate. Steady-state kinetics of ArsC mutants gives a view of the crucial residues for catalysis. ArsC combines a phosphatase-like nucleophilic displacement reaction with a unique intramolecular disulfide bond cascade. Within this cascade, the formation of a disulfide bond triggers a reversible "conformational switch" that transfers the oxidative equivalents to the surface of the protein, while releasing the reduced substrate.
PDB ID: 1LJUDownload
MMDB ID: 20237
PDB Deposition Date: 2002/4/22
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.4  Å
Source Organism:
Similar Structures:
Biological Unit for 1LJU: monomeric; determined by author
Molecular Components in 1LJU
Label Count Molecule
Protein (1 molecule)
Arsenate Reductase(Gene symbol: arsC)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB