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1umk

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(New page: 200px<br /> <applet load="1umk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1umk, resolution 1.75&Aring;" /> '''The Structure of Hu...)
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[[Image:1umk.gif|left|200px]]<br />
 
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<applet load="1umk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1umk, resolution 1.75&Aring;" />
 
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'''The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase'''<br />
 
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==Overview==
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==The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase==
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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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<StructureSection load='1umk' size='340' side='right'caption='[[1umk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1umk]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1UMK FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1umk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umk OCA], [https://pdbe.org/1umk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umk RCSB], [https://www.ebi.ac.uk/pdbsum/1umk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umk ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/NB5R3_HUMAN NB5R3_HUMAN] Recessive hereditary methemoglobinemia type 2;Recessive hereditary methemoglobinemia type 1. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/NB5R3_HUMAN NB5R3_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/main_output.php?pdb_ID=1umk 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 [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://ispc.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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15502298 15502298]
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</div>
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[[Category: Cytochrome-b5 reductase]]
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<div class="pdbe-citations 1umk" style="background-color:#fffaf0;"></div>
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[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Bando, S.]]
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[[Category: Horii, C.]]
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[[Category: Nakagawa, A.]]
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[[Category: Shirabe, K.]]
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[[Category: Takano, T.]]
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[[Category: Takeshita, M.]]
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[[Category: Yubisui, T.]]
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[[Category: FAD]]
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[[Category: beta barrel]]
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[[Category: fad-binding domain]]
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[[Category: flavoprotein]]
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[[Category: nadh-binding domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:36:24 2007''
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==See Also==
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*[[NADH-cytochrome b5 reductase|NADH-cytochrome b5 reductase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Bando S]]
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[[Category: Horii C]]
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[[Category: Nakagawa A]]
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[[Category: Shirabe K]]
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[[Category: Takano T]]
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[[Category: Takeshita M]]
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[[Category: Yubisui T]]

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The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase

PDB ID 1umk

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