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| - | [[Image:1umk.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1umk| PDB=1umk | SCENE= }} | | {{STRUCTURE_1umk| PDB=1umk | SCENE= }} |
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| - | '''The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase'''
| + | ===The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase=== |
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| - | ==Overview==
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| - | 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. |
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| | + | {{ABSTRACT_PUBMED_15502298}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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'' |
Revision as of 20:42, 27 July 2008
Template:STRUCTURE 1umk
The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase
Template:ABSTRACT PUBMED 15502298
About this Structure
1UMK is a Single protein structure of sequence from Homo sapiens. 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
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