1umk: Difference between revisions
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New page: left|200px<br /> <applet load="1umk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1umk, resolution 1.75Å" /> '''The Structure of Hu... |
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[[Image:1umk.gif|left|200px]]<br /> | [[Image:1umk.gif|left|200px]]<br /><applet load="1umk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1umk" size=" | |||
caption="1umk, resolution 1.75Å" /> | caption="1umk, resolution 1.75Å" /> | ||
'''The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase'''<br /> | '''The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase'''<br /> | ||
==Overview== | ==Overview== | ||
Erythrocyte NADH-cytochrome b(5) reductase reduces methaemoglobin to | 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== | ==About this Structure== | ||
1UMK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-b5_reductase Cytochrome-b5 reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.2 1.6.2.2] Full crystallographic information is available from [http:// | 1UMK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-b5_reductase Cytochrome-b5 reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.2 1.6.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMK OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: nadh-binding domain]] | [[Category: nadh-binding domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:09 2008'' | ||
