1hdo: Difference between revisions

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[[Category: methaemoglobin reductase]]
[[Category: methaemoglobin reductase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:02:49 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:34:46 2007''

Revision as of 16:30, 30 October 2007

File:1hdo.gif


1hdo, resolution 1.15Å

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HUMAN BILIVERDIN IX BETA REDUCTASE: NADP COMPLEX

OverviewOverview

Biliverdin IXbeta reductase (BVR-B) catalyzes the pyridine, nucleotide-dependent production of bilirubin-IXbeta, the major heme, catabolite during early fetal development. BVR-B displays a preference for, biliverdin isomers without propionates straddling the C10 position, in, contrast to biliverdin IXalpha reductase (BVR-A), the major form of BVR in, adult human liver. In addition to its tetrapyrrole clearance role in the, fetus, BVR-B has flavin and ferric reductase activities in the adult. We, have solved the structure of human BVR-B in complex with NADP+ at 1.15 A, resolution. Human BVR-B is a monomer displaying an alpha/beta dinucleotide, binding fold. The structures of ternary complexes with mesobiliverdin, IValpha, biliverdin IXalpha, FMN and lumichrome show that human BVR-B has, a ... [(full description)]

About this StructureAbout this Structure

1HDO is a [Single protein] structure of sequence from [Homo sapiens] with NAP as [ligand]. Active as [Biliverdin reductase], with EC number [1.3.1.24]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme., Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M, Nat Struct Biol. 2001 Mar;8(3):215-20. PMID:11224564

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OCA