1LJU

X-RAY STRUCTURE OF C15A ARSENATE REDUCTASE FROM PI258 COMPLEXED WITH ARSENITE

Summary for 1LJU

• Entry DOI: 10.2210/pdb1lju/pdb
• Related: 1JF8 1LJL 1LK0
• Descriptor: arsenate reductase, POTASSIUM ION (3 entities in total)
• Functional Keywords: ptpase i fold, p-loop, oxidoreductase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 14962.70

Authors

Zegers, I.,Martins, J.C.,Willem, R.,Wyns, L.,Messens, J. (deposition date: 2002-04-22, release date: 2002-08-07, Last modification date: 2024-11-06)

Primary citation

Messens, J.,Martins, J.C.,Van Belle, K.,Brosens, E.,Desmyter, A.,De Gieter, M.,Wieruszeski, J.M.,Willem, R.,Wyns, L.,Zegers, I.
All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.
Proc.Natl.Acad.Sci.USA, 99:8506-8511, 2002

PubMed Abstract: 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.

PubMed: 12072565
DOI: 10.1073/pnas.132142799

Experimental method

X-RAY DIFFRACTION (1.4 Å)