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| | <StructureSection load='1gwj' size='340' side='right'caption='[[1gwj]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1gwj' size='340' side='right'caption='[[1gwj]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gwj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GWJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gwj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GWJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 2.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwj OCA], [http://pdbe.org/1gwj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gwj RCSB], [http://www.ebi.ac.uk/pdbsum/1gwj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gwj ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></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=1gwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwj OCA], [https://pdbe.org/1gwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gwj RCSB], [https://www.ebi.ac.uk/pdbsum/1gwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gwj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q51990_PSEPU Q51990_PSEPU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens putidus flugge 1886]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barna, T M]] | + | [[Category: Pseudomonas putida]] |
| - | [[Category: Moody, P C.E]] | + | [[Category: Barna TM]] |
| - | [[Category: Beta/alpha barrel]] | + | [[Category: Moody PCE]] |
| - | [[Category: Flavoenzyme]]
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| - | [[Category: Opiate metabolism]]
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| - | [[Category: Oxido-reducatase]]
| + | |
| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
Q51990_PSEPU
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
The crystal structure of the NADH-dependent bacterial flavoenzyme morphinone reductase (MR) has been determined at 2.2-A resolution in complex with the oxidizing substrate codeinone. The structure reveals a dimeric enzyme comprising two 8-fold beta/alpha barrel domains, each bound to FMN, and a subunit folding topology and mode of flavin-binding similar to that found in Old Yellow Enzyme (OYE) and pentaerythritol tetranitrate (PETN) reductase. The subunit interface of MR is formed by interactions from an N-terminal beta strand and helices 2 and 8 of the barrel domain and is different to that seen in OYE. The active site structures of MR, OYE, and PETN reductase are highly conserved reflecting the ability of these enzymes to catalyze "generic" reactions such as the reduction of 2-cyclohexenone. A region of polypeptide presumed to define the reducing coenzyme specificity is identified by comparison of the MR structure (NADH-dependent) with that of PETN reductase (NADPH-dependent). The active site acid identified in OYE (Tyr-196) and conserved in PETN reductase (Tyr-186) is replaced by Cys-191 in MR. Mutagenesis studies have established that Cys-191 does not act as a crucial acid in the mechanism of reduction of the olefinic bond found in 2-cyclohexenone and codeinone.
Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme.,Barna T, Messiha HL, Petosa C, Bruce NC, Scrutton NS, Moody PC J Biol Chem. 2002 Aug 23;277(34):30976-83. Epub 2002 Jun 4. PMID:12048188[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barna T, Messiha HL, Petosa C, Bruce NC, Scrutton NS, Moody PC. Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme. J Biol Chem. 2002 Aug 23;277(34):30976-83. Epub 2002 Jun 4. PMID:12048188 doi:10.1074/jbc.M202846200
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