1umk
From Proteopedia
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The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase
Overview
Erythrocyte NADH-cytochrome b(5) reductase reduces methaemoglobin to, functional haemoglobin. In order to examine the function of the enzyme, the structure of NADH-cytochrome b(5) reductase from human erythrocytes, has been determined and refined by X-ray crystallography. At 1.75 A, resolution, the root-mean-square deviations (r.m.s.d.) from standard bond, lengths and angles are 0.006 A and 1.03 degrees , respectively. The, molecular structure was compared with those of rat NADH-cytochrome b(5), reductase and corn nitrate reductase. The human reductase resembles the, rat reductase in overall structure as well as in many side chains., Nevertheless, there is a large main-chain shift from the human reductase, to the rat reductase or the corn reductase caused by a single-residue, replacement from proline to threonine. A model of the complex between, cytochrome b(5) and the human reductase has been built and compared with, that of the haem-containing domain of the nitrate reductase molecule. The, interaction between cytochrome b(5) and the human reductase differs from, that of the nitrate reductase because of differences in the amino-acid, sequences. The structures around 15 mutation sites of the human reductase, have been examined for the influence of residue substitutions using the, program ROTAMER. Five mutations in the FAD-binding domain seem to be, related to cytochrome b(5).
About this Structure
1UMK is a Single protein structure of sequence from Homo sapiens with FAD as ligand. Active as Cytochrome-b5 reductase, with EC number 1.6.2.2 Full crystallographic information is available from OCA.
Reference
Structure of human erythrocyte NADH-cytochrome b5 reductase., Bando S, Takano T, Yubisui T, Shirabe K, Takeshita M, Nakagawa A, Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):1929-34. Epub 2004, Oct 20. PMID:15502298
Page seeded by OCA on Mon Nov 12 19:36:24 2007
