1z2d: Difference between revisions

Revision as of 09:35, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1z2d.png

Template:STRUCTURE 1z2d

Solution Structure of Bacillus subtilis ArsC in reduced stateSolution Structure of Bacillus subtilis ArsC in reduced state

Template:ABSTRACT PUBMED 16192272

About this StructureAbout this Structure

1Z2D is a Single protein structure of sequence from Bacillus subtilis. Full experimental information is available from OCA.

ReferenceReference

Solution structures and backbone dynamics of arsenate reductase from Bacillus subtilis: reversible conformational switch associated with arsenate reduction., Guo X, Li Y, Peng K, Hu Y, Li C, Xia B, Jin C, J Biol Chem. 2005 Nov 25;280(47):39601-8. Epub 2005 Sep 28. PMID:16192272

Page seeded by OCA on Tue Jul 29 09:35:48 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1z2d.gif|left|200px]]
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-'''Solution Structure of Bacillus subtilis ArsC in reduced state'''
+===Solution Structure of Bacillus subtilis ArsC in reduced state===
-==Overview==
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-Arsenate reductase encoded by the chromosomal arsC gene in Bacillus subtilis catalyzes the intracellular reduction of arsenate to arsenite, which is then extruded from cells through an efficient and specific transport system. Herein, we present the solution structures and backbone dynamics of both the reduced and oxidized forms of arsenate reductase from B. subtilis. The overall structures of both forms are similar to those of bovine low molecular weight protein-tyrosine phosphatase and arsenate reductase from Staphylococcus aureus. However, several features of the tertiary structure and mobility are notably different between the reduced and oxidized forms of B. subtilis arsenate reductase, particularly in the P-loop region and the segment Cys(82)-Cys(89). The backbone dynamics results demonstrated that the reduced form of arsenate reductase undergoes millisecond conformational changes in the functional P-loop and Cys(82)-Cys(89), which may facilitate the formation of covalent intermediates and subsequent reduction of arsenate. In the oxidized form, Cys(82)-Cys(89) shows motional flexibility on both picosecond-to-nanosecond and possibly millisecond time scales, which may facilitate the reduction of the oxidized enzyme by thioredoxin to regenerate the active enzyme. Overall, the internal dynamics and static structures of the enzyme provide insights into the molecular mechanism of arsenate reduction, especially the reversible conformational switch and changes in internal motions associated with the catalytic reaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_16192272}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16192272}}
 ==About this Structure==
-Z2D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2D OCA].
+Z2D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2D OCA].
 ==Reference==
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 [[Category: Solution structure]]
 [[Category: Structural genomic]]
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