1jl3
From Proteopedia
(New page: 200px<br /><applet load="1jl3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jl3, resolution 1.60Å" /> '''Crystal Structure of...) |
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| - | [[Image:1jl3.jpg|left|200px]]<br /><applet load="1jl3" size=" | + | [[Image:1jl3.jpg|left|200px]]<br /><applet load="1jl3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jl3, resolution 1.60Å" /> | caption="1jl3, resolution 1.60Å" /> | ||
'''Crystal Structure of B. subtilis ArsC'''<br /> | '''Crystal Structure of B. subtilis ArsC'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Arsenate is an abundant oxyanion that, because of its ability to mimic the | + | Arsenate is an abundant oxyanion that, because of its ability to mimic the phosphate group, is toxic to cells. Arsenate reductase (EC; encoded by the arsC gene in bacteria) participates to achieve arsenate resistance in both prokaryotes and yeast by reducing arsenate to arsenite; the arsenite is then exported by a specific transporter. The crystal structure of Bacillus subtilis arsenate reductase in the reduced form with a bound sulfate ion in its active site is solved at 1.6-A resolution. Significant structural similarity is seen between arsenate reductase and bovine low molecular weight protein tyrosine phosphatase, despite very low sequence identity. The similarity is especially high between their active sites. It is further confirmed that this structural homology is relevant functionally by showing the phosphatase activity of the arsenate reductase in vitro. Thus, we can understand the arsenate reduction in the light of low molecular weight protein tyrosine phosphatase mechanism and also explain the catalytic roles of essential residues such as Cys-10, Cys-82, Cys-89, Arg-16, and Asp-105. A "triple cysteine redox relay" is proposed for the arsenate reduction mechanism. |
==About this Structure== | ==About this Structure== | ||
| - | 1JL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JL3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bennett, M | + | [[Category: Bennett, M S.]] |
| - | [[Category: Su, X | + | [[Category: Su, X D.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: alpha-beta fold]] | [[Category: alpha-beta fold]] | ||
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[[Category: ptp-loop]] | [[Category: ptp-loop]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:53 2008'' |
Revision as of 11:23, 21 February 2008
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Crystal Structure of B. subtilis ArsC
Overview
Arsenate is an abundant oxyanion that, because of its ability to mimic the phosphate group, is toxic to cells. Arsenate reductase (EC; encoded by the arsC gene in bacteria) participates to achieve arsenate resistance in both prokaryotes and yeast by reducing arsenate to arsenite; the arsenite is then exported by a specific transporter. The crystal structure of Bacillus subtilis arsenate reductase in the reduced form with a bound sulfate ion in its active site is solved at 1.6-A resolution. Significant structural similarity is seen between arsenate reductase and bovine low molecular weight protein tyrosine phosphatase, despite very low sequence identity. The similarity is especially high between their active sites. It is further confirmed that this structural homology is relevant functionally by showing the phosphatase activity of the arsenate reductase in vitro. Thus, we can understand the arsenate reduction in the light of low molecular weight protein tyrosine phosphatase mechanism and also explain the catalytic roles of essential residues such as Cys-10, Cys-82, Cys-89, Arg-16, and Asp-105. A "triple cysteine redox relay" is proposed for the arsenate reduction mechanism.
About this Structure
1JL3 is a Single protein structure of sequence from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.
Reference
Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases., Bennett MS, Guan Z, Laurberg M, Su XD, Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13577-82. Epub 2001 Nov 6. PMID:11698660
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