1dms
From Proteopedia
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- | [[Image:1dms.gif|left|200px]] | + | [[Image:1dms.gif|left|200px]] |
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- | '''STRUCTURE OF DMSO REDUCTASE''' | + | {{Structure |
+ | |PDB= 1dms |SIZE=350|CAPTION= <scene name='initialview01'>1dms</scene>, resolution 1.88Å | ||
+ | |SITE= <scene name='pdbsite=MOL:Di+Oxo+Mo+Center+Of+Cofactor'>MOL</scene> and <scene name='pdbsite=PGD:Q-Mgd+Of+Cofactor'>PGD</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</scene> and <scene name='pdbligand=MM4:MOLYBDENUM (IV) OXIDE'>MM4</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE OF DMSO REDUCTASE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1DMS is a [ | + | 1DMS is a [[Single protein]] structure of 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=1DMS OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution., Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein J, J Mol Biol. 1996 Oct 18;263(1):53-69. PMID:[http:// | + | Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution., Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein J, J Mol Biol. 1996 Oct 18;263(1):53-69. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8890912 8890912] |
[[Category: Rhodobacter capsulatus]] | [[Category: Rhodobacter capsulatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: molydopterin]] | [[Category: molydopterin]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:40:59 2008'' |
Revision as of 08:41, 20 March 2008
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, resolution 1.88Å | |||||||
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Sites: | and | ||||||
Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE OF DMSO REDUCTASE
Overview
The periplasmic dimethyl sulfoxide reductase (DMSOR) from the photosynthetic purple bacterium Rhodobacter capsulatus functions as the terminal electron acceptor in its respiratory chain. The enzyme catalyzes the reduction of highly oxidized substrates like dimethyl sulfoxide to dimethyl sulfide. At a molybdenum redox center, two single electrons are transferred from cytochrome C556 to the substrate dimethyl sulfoxide, generating dimethyl sulfide and (with two protons) water. The enzyme was purified and crystallized in space group P4(1)2(1)2 with unit cell dimensions of a = b = 80.7 A and c = 229.2 A. The crystals diffract beyond 1.8 A with synchrotron radiation. The three-dimensional structure was solved by a combination of multiple isomorphous replacement and molecular replacement techniques. The atomic model was refined to an R-factor of 0.169 for 57,394 independent reflections. The spherical protein consists of four domains with a funnel-like cavity that leads to the freely accessible metal-ion redox center. The bis(molybdopterin guanine dinucleotide) molybdenum cofactor (1541 Da) of the single chain protein (85,033 Da) has the molybdenum ion bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule. Three additional ligands, two oxo groups and the oxygen of a serine side-chain, are bound to the molybdenum ion. The second molybdopterin system is not part of the ligand sphere of the metal center with its sulfur atoms at distances of 3.5 A and 3.8 A away. It might be involved in electron shuttling from the protein surface to the molybdenum center.
About this Structure
1DMS is a Single protein structure of sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA.
Reference
Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution., Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein J, J Mol Biol. 1996 Oct 18;263(1):53-69. PMID:8890912
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