1e18: Difference between revisions
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[[Image:1e18.gif|left|200px]]<br /> | [[Image:1e18.gif|left|200px]]<br /><applet load="1e18" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1e18" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1e18, resolution 2.0Å" /> | caption="1e18, resolution 2.0Å" /> | ||
'''TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS'''<br /> | '''TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1E18 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with PGD, 6WO and EOH as [http://en.wikipedia.org/wiki/ligands ligands]. | 1E18 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with PGD, 6WO and EOH as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=ACT:Active Site'>ACT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E18 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tungsten]] | [[Category: tungsten]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:50:38 2007'' | ||
Revision as of 12:40, 18 December 2007
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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 PGD, 6WO and EOH as ligands. Known structural/functional Site: ACT. 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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