1gcu
From Proteopedia
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| - | [[Image:1gcu.jpg|left|200px]] | + | [[Image:1gcu.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A''' | + | {{Structure |
| + | |PDB= 1gcu |SIZE=350|CAPTION= <scene name='initialview01'>1gcu</scene>, resolution 1.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GCU is a [ | + | 1GCU is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11224565 11224565] |
[[Category: Biliverdin reductase]] | [[Category: Biliverdin reductase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''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 11:21:27 2008'' |
Revision as of 09:21, 20 March 2008
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| , resolution 1.4Å | |||||||
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| Activity: | Biliverdin reductase, with EC number 1.3.1.24 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A
Overview
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.
About this Structure
1GCU is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
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