1LJL
Wild Type pI258 S. aureus arsenate reductase
Summary for 1LJL
Entry DOI | 10.2210/pdb1ljl/pdb |
Related | 1JF8 1LJU 1LK0 |
Descriptor | arsenate reductase, POTASSIUM ION (3 entities in total) |
Functional Keywords | p-loop, oxidoreductase |
Biological source | Staphylococcus aureus |
Cellular location | Cytoplasm : P0A006 |
Total number of polymer chains | 1 |
Total formula weight | 14870.84 |
Authors | Messens, J.,Martins, J.C.,Van Belle, K.,Brosens, E.,Desmyter, A.,De Gieter, M.,Wieruszeski, J.M.,Willem, R.,Wyns, L.,Zegers, I. (deposition date: 2002-04-21, release date: 2002-08-07, Last modification date: 2023-08-16) |
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 Cited by 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: 12072565DOI: 10.1073/pnas.132142799 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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