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1e18

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Revision as of 08:40, 16 October 2019

TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS

Structural highlights

1e18 is a 1 chain structure with sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1dmr, 2dmr, 3dmr, 4dmr
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DSTOR_RHOCA] Catalyzes the reduction of dimethyl sulfoxide (DMSO) and trimethylamine N-oxide (TMAO) to dimethyl sulfide (DMS) and trimethylamine, respectively. The terminal DMSO reductase can also use various sulfoxides and N-oxide compounds as terminal electron acceptor in addition to DMSO and TMAO.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ McEwan AG, Ferguson SJ, Jackson JB. Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme. Biochem J. 1991 Feb 15;274 ( Pt 1):305-7. PMID:2001248
↑ Shaw AL, Hanson GR, McEwan AG. Cloning and sequence analysis of the dimethylsulfoxide reductase structural gene from Rhodobacter capsulatus. Biochim Biophys Acta. 1996 Sep 30;1276(3):176-80. PMID:8856102
↑ Stewart LJ, Bailey S, Bennett B, Charnock JM, Garner CD, McAlpine AS. Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site. J Mol Biol. 2000 Jun 9;299(3):593-600. PMID:10835270 doi:10.1006/jmbi.2000.3702

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e18"

@@ Line 1: / Line 1: @@
 ==TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS==
-<StructureSection load='1e18' size='340' side='right' caption='[[1e18]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1e18' size='340' side='right'caption='[[1e18]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1e18]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E18 FirstGlance]. <br>
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Rhodobacter capsulatus]]
 [[Category: Bailey, S]]

1e18

From Proteopedia

Revision as of 08:40, 16 October 2019

TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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