1eu1: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1eu1' size='340' side='right'caption='[[1eu1]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='1eu1' size='340' side='right'caption='[[1eu1]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1eu1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"luteovulum_sphaeroides"_(van_niel_1944)_suresh_et_al._2019 "luteovulum sphaeroides" (van niel 1944) suresh et al. 2019]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cxs 1cxs] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cxt 1cxt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EU1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1eu1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cxs 1cxs] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cxt 1cxt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EU1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6MO:MOLYBDENUM(VI)+ION'>6MO</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6MO:MOLYBDENUM(VI)+ION'>6MO</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cxs|1cxs]], [[1cxt|1cxt]]</div></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eu1 OCA], [https://pdbe.org/1eu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eu1 RCSB], [https://www.ebi.ac.uk/pdbsum/1eu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eu1 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eu1 OCA], [https://pdbe.org/1eu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eu1 RCSB], [https://www.ebi.ac.uk/pdbsum/1eu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eu1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DSTOR_RHOSH DSTOR_RHOSH]] 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.<ref>PMID:9401017</ref>
[https://www.uniprot.org/uniprot/DSTOR_CERSP DSTOR_CERSP] 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.<ref>PMID:9401017</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 25: Line 24:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cereibacter sphaeroides]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Li, H K]]
[[Category: Li HK]]
[[Category: Rajagopalan, K V]]
[[Category: Rajagopalan KV]]
[[Category: Schindelin, H]]
[[Category: Schindelin H]]
[[Category: Temple, K]]
[[Category: Temple K]]
[[Category: Dmso]]
[[Category: Mgd]]
[[Category: Molybdenum]]
[[Category: Molybdenum cofactor]]
[[Category: Molybdopterin]]
[[Category: Oxidoreductase]]
[[Category: Reductase]]

Latest revision as of 13:06, 20 March 2024

THE CRYSTAL STRUCTURE OF RHODOBACTER SPHAEROIDES DIMETHYLSULFOXIDE REDUCTASE REVEALS TWO DISTINCT MOLYBDENUM COORDINATION ENVIRONMENTS.THE CRYSTAL STRUCTURE OF RHODOBACTER SPHAEROIDES DIMETHYLSULFOXIDE REDUCTASE REVEALS TWO DISTINCT MOLYBDENUM COORDINATION ENVIRONMENTS.

Structural highlights

1eu1 is a 1 chain structure with sequence from Cereibacter sphaeroides. This structure supersedes the now removed PDB entries 1cxs and 1cxt. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.3Å
Ligands:, , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DSTOR_CERSP 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]

Evolutionary Conservation

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

References

  1. ↑ Mouncey NJ, Choudhary M, Kaplan S. Characterization of genes encoding dimethyl sulfoxide reductase of Rhodobacter sphaeroides 2.4.1T: an essential metabolic gene function encoded on chromosome II. J Bacteriol. 1997 Dec;179(24):7617-24. PMID:9401017

1eu1, resolution 1.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1eu1&oldid=4108361"