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1e18

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==Overview==
==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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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.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bailey, S.]]
[[Category: Bailey, S.]]
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[[Category: Stewart, L.J.]]
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[[Category: Stewart, L J.]]
[[Category: 6WO]]
[[Category: 6WO]]
[[Category: EOH]]
[[Category: EOH]]
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[[Category: tungsten]]
[[Category: tungsten]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:36:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:40 2008''

Revision as of 10:22, 21 February 2008


1e18, resolution 2.0Å

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TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS

Overview

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.

About this Structure

1E18 is a Single protein structure of sequence from Rhodobacter capsulatus with , and as ligands. Known structural/functional Site: . 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

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