1E18

TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS

Summary for 1E18

• Entry DOI: 10.2210/pdb1e18/pdb
• Related: 1DMR 2DMR 3DMR 4DMR
• Descriptor: DMSO REDUCTASE., 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE, OXO-TUNGSTEN(VI), ... (5 entities in total)
• Functional Keywords: oxidoreductase, reductase, dmso, molybdopterin, molybdenum, tungsten
• Biological source: RHODOBACTER CAPSULATUS
• Cellular location: Periplasm: Q52675
• Total number of polymer chains: 1
• Total formula weight: 91398.18

Authors

Bailey, S.,Stewart, L.J. (deposition date: 2000-04-28, release date: 2000-06-11, Last modification date: 2024-05-08)

Primary citation

Stewart, L.J.,Bailey, S.,Bennett, B.,Charnock, J.M.,Garner, C.D.,Mcalpine, A.S.
Dimethylsulfoxide Reductase: An Enzyme Capable of Catalysis with Either Molybdenum or Tungsten at the Active Site
J.Mol.Biol., 299:593-, 2000

PubMed Abstract: 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.

PubMed: 10835270
DOI: 10.1006/JMBI.2000.3702

Experimental method

X-RAY DIFFRACTION (2 Å)