1e18

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[[Image:1e18.gif|left|200px]]
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{{Seed}}
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[[Image:1e18.png|left|200px]]
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{{STRUCTURE_1e18| PDB=1e18 | SCENE= }}
{{STRUCTURE_1e18| PDB=1e18 | SCENE= }}
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'''TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS'''
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===TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS===
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==Overview==
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DMSO reductase (DMSOR) from Rhodobacter capsulatus, well-characterised as a molybdoenzyme, will bind tungsten. Protein crystallography has shown that tungsten in W-DMSOR is ligated by the dithiolene group of the two pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is located in a very similar site to that of molybdenum in Mo-DMSOR. These conclusions are consistent with W L(III)-edge X-ray absorption, EPR and UV/visible spectroscopic data. W-DMSOR is significantly more active than Mo-DMSOR in catalysing the reduction of DMSO but, in contrast to the latter, shows no significant ability to catalyse the oxidation of DMS.
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The line below this paragraph, {{ABSTRACT_PUBMED_10835270}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 10835270 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10835270}}
==About this Structure==
==About this Structure==
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[[Category: Reductase]]
[[Category: Reductase]]
[[Category: Tungsten]]
[[Category: Tungsten]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:31:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:58:23 2008''

Revision as of 20:58, 30 June 2008

Image:1e18.png

Template:STRUCTURE 1e18

TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS

Template:ABSTRACT PUBMED 10835270

About this Structure

1E18 is a Single protein structure of sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA.

Reference

Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site., Stewart LJ, Bailey S, Bennett B, Charnock JM, Garner CD, McAlpine AS, J Mol Biol. 2000 Jun 9;299(3):593-600. PMID:10835270

Page seeded by OCA on Mon Jun 30 23:58:23 2008

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