1s3c

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[[Image:1s3c.gif|left|200px]]
[[Image:1s3c.gif|left|200px]]
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{{Structure
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|PDB= 1s3c |SIZE=350|CAPTION= <scene name='initialview01'>1s3c</scene>, resolution 1.25&Aring;
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The line below this paragraph, containing "STRUCTURE_1s3c", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1s3c| PDB=1s3c | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3c OCA], [http://www.ebi.ac.uk/pdbsum/1s3c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s3c RCSB]</span>
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'''ARSENATE REDUCTASE C12S MUTANT FROM E. COLI'''
'''ARSENATE REDUCTASE C12S MUTANT FROM E. COLI'''
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==Reference==
==Reference==
Arginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) product., DeMel S, Shi J, Martin P, Rosen BP, Edwards BF, Protein Sci. 2004 Sep;13(9):2330-40. Epub 2004 Aug 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15295115 15295115]
Arginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) product., DeMel S, Shi J, Martin P, Rosen BP, Edwards BF, Protein Sci. 2004 Sep;13(9):2330-40. Epub 2004 Aug 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15295115 15295115]
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[[Category: Arsenate reductase (glutaredoxin)]]
 
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: DeMel, S.]]
[[Category: DeMel, S.]]
[[Category: Edwards, B F.]]
[[Category: Edwards, B F.]]
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[[Category: arsc]]
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[[Category: Arsc]]
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[[Category: arsenate]]
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[[Category: Arsenate]]
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[[Category: arsenite]]
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[[Category: Arsenite]]
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[[Category: reductase]]
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[[Category: Reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:14:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:36:46 2008''
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Revision as of 05:14, 3 May 2008

Image:1s3c.gif

Template:STRUCTURE 1s3c

ARSENATE REDUCTASE C12S MUTANT FROM E. COLI


Overview

Arsenic is a ubiquitous environmental toxic metal. Consequently, organisms detoxify arsenate by reduction to arsenite, which is then excreted or sequestered. The ArsC arsenate reductase from Escherichia coli plasmid R773, the best characterized arsenic-modifying enzyme, has a catalytic cysteine, Cys 12, in the active site, surrounded by an arginine triad composed of Arg 60, Arg 94, and Arg 107. During the reaction cycle, the native enzyme forms a unique monohydroxyl Cys 12-thiol-arsenite adduct that contains a positive charge on the arsenic. We hypothesized previously that this unstable intermediate allows for rapid dissociation of the product arsenite. In this study, the role of Arg 60 in product formation was evaluated by mutagenesis. A total of eight new structures of ArsC were determined at resolutions between 1.3 A and 1.8 A, with R(free) values between 0.18 and 0.25. The crystal structures of R60K and R60A ArsC equilibrated with the product arsenite revealed a covalently bound Cys 12-thiol-dihydroxyarsenite without a charge on the arsenic atom. We propose that this intermediate is more stable than the monohydroxyarsenite intermediate of the native enzyme, resulting in slow release of product and, consequently, loss of activity.

About this Structure

1S3C is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Arginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) product., DeMel S, Shi J, Martin P, Rosen BP, Edwards BF, Protein Sci. 2004 Sep;13(9):2330-40. Epub 2004 Aug 4. PMID:15295115 Page seeded by OCA on Sat May 3 08:14:44 2008

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