1e18: Difference between revisions
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|PDB= 1e18 |SIZE=350|CAPTION= <scene name='initialview01'>1e18</scene>, resolution 2.0Å | |PDB= 1e18 |SIZE=350|CAPTION= <scene name='initialview01'>1e18</scene>, resolution 2.0Å | ||
|SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene> | |SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene> | ||
|LIGAND= <scene name='pdbligand=PGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>PGD | |LIGAND= <scene name='pdbligand=6WO:OXO-TUNGSTEN(VI)'>6WO</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=PGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>PGD</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e18 OCA], [http://www.ebi.ac.uk/pdbsum/1e18 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e18 RCSB]</span> | |||
}} | }} | ||
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[[Category: Bailey, S.]] | [[Category: Bailey, S.]] | ||
[[Category: Stewart, L J.]] | [[Category: Stewart, L J.]] | ||
[[Category: dmso]] | [[Category: dmso]] | ||
[[Category: molybdenum]] | [[Category: molybdenum]] | ||
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[[Category: tungsten]] | [[Category: tungsten]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:58 2008'' | ||
Revision as of 16:52, 30 March 2008
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| 1e18, resolution 2.0Å | |||||||||||||
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| Sites: | ACT | ||||||||||||
| Ligands: | 6WO, EOH, PGD | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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