1lju
From Proteopedia
(New page: 200px<br /><applet load="1lju" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lju, resolution 1.4Å" /> '''X-RAY STRUCTURE OF C1...) |
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| - | [[Image:1lju.jpg|left|200px]]<br /><applet load="1lju" size=" | + | [[Image:1lju.jpg|left|200px]]<br /><applet load="1lju" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lju, resolution 1.4Å" /> | caption="1lju, resolution 1.4Å" /> | ||
'''X-RAY STRUCTURE OF C15A ARSENATE REDUCTASE FROM PI258 COMPLEXED WITH ARSENITE'''<br /> | '''X-RAY STRUCTURE OF C15A ARSENATE REDUCTASE FROM PI258 COMPLEXED WITH ARSENITE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The mechanism of pI258 arsenate reductase (ArsC) catalyzed arsenate | + | 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== | ==About this Structure== | ||
| - | 1LJU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] Full crystallographic information is available from [http:// | + | 1LJU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| - | [[Category: Martins, J | + | [[Category: Martins, J C.]] |
[[Category: Messens, J.]] | [[Category: Messens, J.]] | ||
[[Category: Willem, R.]] | [[Category: Willem, R.]] | ||
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[[Category: ptpase i fold]] | [[Category: ptpase i fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:33 2008'' |
Revision as of 11:45, 21 February 2008
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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
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