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1he3

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Revision as of 11:42, 30 October 2007 by OCA (Talk | contribs)
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Image:1he3.gif

1he3, resolution 1.40Å

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HUMAN BILIVERDIN IX BETA REDUCTASE: NADP/MESOBILIVERDIN IV ALPHA TERNARY COMPLEX

Overview

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 Structure

1HE3 is a [Single protein] structure of sequence from [Homo sapiens] with NAP and MBV as [ligands]. Active as [Biliverdin reductase], with EC number [1.3.1.24]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [OCA].

Reference

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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