Back to Search
Start Over
Structure of human erythrocyte NADH-cytochrome b5 reductase.
- Source :
-
Acta Crystallographica: Section D (Wiley-Blackwell) . Nov2004, Vol. 60 Issue 11, p1929-1934. 6p. - Publication Year :
- 2004
-
Abstract
- Erythrocyte NADH-cytochrome b5 reductase reduces methaemoglobin to functional haemoglobin. In order to examine the function of the enzyme, the structure of NADH-cytochrome b5 reductase from human erythrocytes has been determined and refined by X-ray crystallography. At 1.75 Å resolution, the root-mean-square deviations (r.m.s.d.) from standard bond lengths and angles are 0.006 Å and 1.03°, respectively. The molecular structure was compared with those of rat NADH-cytochrome b5 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 b5 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 b5 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 b5. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09074449
- Volume :
- 60
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section D (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 14797655
- Full Text :
- https://doi.org/10.1107/S0907444904020645