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| | {{STRUCTURE_1lc0| PDB=1lc0 | SCENE= }} | | {{STRUCTURE_1lc0| PDB=1lc0 | SCENE= }} |
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| - | '''Structure of Biliverdin Reductase and the Enzyme-NADH Complex'''
| + | ===Structure of Biliverdin Reductase and the Enzyme-NADH Complex=== |
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| - | ==Overview==
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| - | Biliverdin reductase (BVR) catalyzes the last step in heme degradation by reducing the gamma-methene bridge of the open tetrapyrrole, biliverdin IXalpha, to bilirubin with the concomitant oxidation of a beta-nicotinamide adenine dinucleotide (NADH) or beta-nicotinamide adenine dinucleotide phosphate (NADPH) cofactor. Bilirubin is the major bile pigment in mammals and has antioxidant and anticompliment activity. We have determined X-ray crystal structures of apo rat BVR and its complex with NADH at 1.2 A and 1.5 A resolution, respectively. In agreement with an independent structure determination of the apo-enzyme, BVR consists of an N-terminal dinucleotide-binding domain (Rossmann-fold) and a C-terminal domain that contains a six-stranded beta-sheet that is flanked on one face by several alpha-helices. The C-terminal and N-terminal domains interact extensively, forming the active site cleft at their interface. The cofactor complex structure reported here reveals that the cofactor nicotinamide ring extends into the active site cleft, where it is adjacent to conserved amino acid residues and, consistent with the known stereochemistry of the reaction catalyzed by BVR, the si face of the ring is accessible for hydride transfer. The only titratable side-chain that appears to be suitably positioned to function as a general acid in catalysis is Tyr97. This residue, however, is not essential for catalysis, since the Tyr97Phe mutant protein retains 50% activity. This finding suggests that the dominant role in catalysis may be performed by hydride transfer from the cofactor, a process that may be promoted by proximity of the invariant residues Glu96, Glu123, and Glu126, to the nicotinamide ring.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12079357}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12079357 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12079357}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| | [[Category: Tetrapyrrole]] | | [[Category: Tetrapyrrole]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:46:29 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:18:10 2008'' |
Revision as of 09:18, 2 July 2008
Template:STRUCTURE 1lc0
Structure of Biliverdin Reductase and the Enzyme-NADH Complex
Template:ABSTRACT PUBMED 12079357
About this Structure
1LC0 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex., Whitby FG, Phillips JD, Hill CP, McCoubrey W, Maines MD, J Mol Biol. 2002 Jun 21;319(5):1199-210. PMID:12079357
Page seeded by OCA on Wed Jul 2 12:18:10 2008
