|
|
| Line 1: |
Line 1: |
| [[Image:1umk.gif|left|200px]] | | {{Seed}} |
| | [[Image:1umk.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1umk| PDB=1umk | SCENE= }} | | {{STRUCTURE_1umk| PDB=1umk | SCENE= }} |
|
| |
|
| '''The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase'''
| | ===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).
| | The line below this paragraph, {{ABSTRACT_PUBMED_15502298}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15502298 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_15502298}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 34: |
Line 38: |
| [[Category: Flavoprotein]] | | [[Category: Flavoprotein]] |
| [[Category: Nadh-binding domain]] | | [[Category: Nadh-binding domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:25:45 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:42:25 2008'' |
