4dmr
From Proteopedia
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| - | [[Image:4dmr. | + | [[Image:4dmr.jpg|left|200px]]<br /><applet load="4dmr" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="4dmr" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="4dmr, resolution 1.90Å" /> | caption="4dmr, resolution 1.90Å" /> | ||
'''REDUCED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS WITH BOUND DMSO SUBSTRATE'''<br /> | '''REDUCED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS WITH BOUND DMSO SUBSTRATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 4DMR 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, 4MO, O and DMS as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 4DMR 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, 4MO, O and DMS as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=MO:The Substrate Dmso Is Bound At The Active Site To The Mo ...'>MO</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4DMR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: substrate bound]] | [[Category: substrate bound]] | ||
| - | ''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 20:43:46 2007'' |
Revision as of 18:33, 18 December 2007
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REDUCED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS WITH BOUND DMSO SUBSTRATE
Overview
The crystal structure of the molybdenum enzyme dimethylsulphoxide, reductase (DMSOR) has been determined at 1.9 A resolution with substrate, bound at the active site. DMSOR is an oxotransferase which catalyses the, reduction of dimethylsulphoxide (DMSO) to dimethylsulphide (DMS) in a two, stage reaction which is linked to oxygen atom transfer and electron, transfer. In the first step, DMSO binds to reduced (Mo(IV)) enzyme, the, enzyme is oxidised to Mo(VI) with an extra oxygen ligand and DMS is, released. Regeneration of reduced enzyme is achieved by transfer of two, electrons, successively from a specific cytochrome, and release of the, oxygen as water. The enzyme, purified under aerobic conditions, is in the, oxidised (Mo(VI)) state. Addition of a large excess of DMS to the oxidised, enzyme in solution causes a change in the absorption spectrum of the, enzyme. The same reaction occurs within crystals of the enzyme and the, crystal structure reveals a complex with DMSO bound to the molybdenum via, its oxygen atom. X-ray edge data indicate that the metal is in the Mo(IV), state. The DMSO ligand replaces one of the two oxo groups which ligate the, oxidised form of the enzyme, suggesting very strongly that this is the, oxygen which is transferred during catalysis. Residues 384 to 390, disordered in the oxidised enzyme, are now clearly seen in the cleft, leading to the active site. The side-chain of Trp388 forms a lid trapping, the substrate/product.
About this Structure
4DMR is a Single protein structure of sequence from Rhodobacter capsulatus with PGD, 4MO, O and DMS as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The high resolution crystal structure of DMSO reductase in complex with DMSO., McAlpine AS, McEwan AG, Bailey S, J Mol Biol. 1998 Jan 30;275(4):613-23. PMID:9466935
Page seeded by OCA on Tue Dec 18 20:43:46 2007
Categories: Rhodobacter capsulatus | Single protein | Bailey, S. | Mcalpine, A.S. | 4MO | DMS | O | PGD | Dmso | Molybdopterin | Oxidoreductase | Substrate bound
