1ljl

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{{STRUCTURE_1ljl| PDB=1ljl | SCENE= }}
{{STRUCTURE_1ljl| PDB=1ljl | SCENE= }}
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'''Wild Type pI258 S. aureus arsenate reductase'''
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===Wild Type pI258 S. aureus arsenate reductase===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12072565 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12072565}}
==About this Structure==
==About this Structure==
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[[Category: Zegers, I.]]
[[Category: Zegers, I.]]
[[Category: P-loop]]
[[Category: P-loop]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:58:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:01:26 2008''

Revision as of 18:01, 2 July 2008

Image:1ljl.png

Template:STRUCTURE 1ljl

Wild Type pI258 S. aureus arsenate reductase

Template:ABSTRACT PUBMED 12072565

About this Structure

1LJL is a Single protein structure of sequence from Staphylococcus aureus. 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 Wed Jul 2 21:01:26 2008

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