1umk

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{{STRUCTURE_1umk| PDB=1umk | SCENE= }}
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==The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase==
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===The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase===
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<StructureSection load='1umk' size='340' side='right' caption='[[1umk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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{{ABSTRACT_PUBMED_15502298}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1umk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UMK FirstGlance]. <br>
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==Disease==
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>
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[[http://www.uniprot.org/uniprot/NCB5R_HUMAN NCB5R_HUMAN]] Defects in CYB5R3 are the cause of methemoglobinemia CYB5R3-related (METHB-CYB5R3) [MIM:[http://omim.org/entry/250800 250800]]. A form of methemoglobinemia, a hematologic disease characterized by the presence of excessive amounts of methemoglobin in blood cells, resulting in decreased oxygen carrying capacity of the blood, cyanosis and hypoxia. There are two types of methemoglobinemia CYB5R3-related. In type 1, the defect affects the soluble form of the enzyme, is restricted to red blood cells, and causes well-tolerated methemoglobinemia. In type 2, the defect affects both the soluble and microsomal forms of the enzyme and is thus generalized, affecting red cells, leukocytes and all body tissues. Type 2 methemoglobinemia is associated with mental deficiency and other neurologic symptoms.<ref>PMID:1898726</ref><ref>PMID:1707593</ref><ref>PMID:1400360</ref><ref>PMID:8119939</ref><ref>PMID:7718898</ref><ref>PMID:9695975</ref><ref>PMID:9886302</ref><ref>PMID:10807796</ref><ref>PMID:15622768</ref><ref>PMID:12393396</ref><ref>PMID:15953014</ref>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1umk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1umk RCSB], [http://www.ebi.ac.uk/pdbsum/1umk PDBsum]</span></td></tr>
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==Function==
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<table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/NCB5R_HUMAN NCB5R_HUMAN]] Defects in CYB5R3 are the cause of methemoglobinemia CYB5R3-related (METHB-CYB5R3) [MIM:[http://omim.org/entry/250800 250800]]. A form of methemoglobinemia, a hematologic disease characterized by the presence of excessive amounts of methemoglobin in blood cells, resulting in decreased oxygen carrying capacity of the blood, cyanosis and hypoxia. There are two types of methemoglobinemia CYB5R3-related. In type 1, the defect affects the soluble form of the enzyme, is restricted to red blood cells, and causes well-tolerated methemoglobinemia. In type 2, the defect affects both the soluble and microsomal forms of the enzyme and is thus generalized, affecting red cells, leukocytes and all body tissues. Type 2 methemoglobinemia is associated with mental deficiency and other neurologic symptoms.<ref>PMID:1898726</ref> <ref>PMID:1707593</ref> <ref>PMID:1400360</ref> <ref>PMID:8119939</ref> <ref>PMID:7718898</ref> <ref>PMID:9695975</ref> <ref>PMID:9886302</ref> <ref>PMID:10807796</ref> <ref>PMID:15622768</ref> <ref>PMID:12393396</ref> <ref>PMID:15953014</ref>
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== Function ==
[[http://www.uniprot.org/uniprot/NCB5R_HUMAN NCB5R_HUMAN]] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
[[http://www.uniprot.org/uniprot/NCB5R_HUMAN NCB5R_HUMAN]] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/um/1umk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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).
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==About this Structure==
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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<ref>PMID:15502298</ref>
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[[1umk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMK OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:015502298</ref><references group="xtra"/><references/>
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Cytochrome-b5 reductase]]
[[Category: Cytochrome-b5 reductase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 21:25, 29 September 2014

The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase

1umk, resolution 1.75Å

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