1lju
From Proteopedia
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X-RAY STRUCTURE OF C15A ARSENATE REDUCTASE FROM PI258 COMPLEXED WITH ARSENITE
Overview
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.
About this Structure
1LJU is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Active as Arsenate reductase (glutaredoxin), with EC number 1.20.4.1 Full crystallographic information is available from OCA.
Reference
All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade., Messens J, Martins JC, Van Belle K, Brosens E, Desmyter A, De Gieter M, Wieruszeski JM, Willem R, Wyns L, Zegers I, Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8506-11. Epub 2002 Jun 18. PMID:12072565
Page seeded by OCA on Thu Feb 21 13:45:33 2008
