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| | <StructureSection load='1gcu' size='340' side='right'caption='[[1gcu]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='1gcu' size='340' side='right'caption='[[1gcu]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gcu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GCU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gcu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GCU FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Biliverdin_reductase Biliverdin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.24 1.3.1.24] </span></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]] 1.4Å</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=1gcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcu OCA], [http://pdbe.org/1gcu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gcu RCSB], [http://www.ebi.ac.uk/pdbsum/1gcu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gcu 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=1gcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcu OCA], [https://pdbe.org/1gcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gcu RCSB], [https://www.ebi.ac.uk/pdbsum/1gcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gcu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BIEA_RAT BIEA_RAT]] Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. | + | [https://www.uniprot.org/uniprot/BIEA_RAT BIEA_RAT] Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. |
| | == 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: Biliverdin reductase]] | |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kikuchi, A]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Park, S Y]] | + | [[Category: Kikuchi A]] |
| - | [[Category: Shiro, Y]] | + | [[Category: Park SY]] |
| - | [[Category: Biliverdin]] | + | [[Category: Shiro Y]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
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| Structural highlights
Function
BIEA_RAT Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.
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
Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 A resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that is predominantly an antiparallel six-stranded beta-sheet. Based on this structure, we propose modes of binding for NAD(P)H and biliverdin, and a possible mechanism for the enzyme.
Crystal structure of rat biliverdin reductase.,Kikuchi A, Park SY, Miyatake H, Sun D, Sato M, Yoshida T, Shiro Y Nat Struct Biol. 2001 Mar;8(3):221-5. PMID:11224565[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kikuchi A, Park SY, Miyatake H, Sun D, Sato M, Yoshida T, Shiro Y. Crystal structure of rat biliverdin reductase. Nat Struct Biol. 2001 Mar;8(3):221-5. PMID:11224565 doi:10.1038/84955
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