1lc0

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(New page: 200px<br /><applet load="1lc0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lc0, resolution 1.20&Aring;" /> '''Structure of Biliver...)
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[[Image:1lc0.jpg|left|200px]]<br /><applet load="1lc0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lc0, resolution 1.20&Aring;" />
 
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'''Structure of Biliverdin Reductase and the Enzyme-NADH Complex'''<br />
 
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==Overview==
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==Structure of Biliverdin Reductase and the Enzyme-NADH Complex==
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Biliverdin reductase (BVR) catalyzes the last step in heme degradation by, reducing the gamma-methene bridge of the open tetrapyrrole, biliverdin, IXalpha, to bilirubin with the concomitant oxidation of a, beta-nicotinamide adenine dinucleotide (NADH) or beta-nicotinamide adenine, dinucleotide phosphate (NADPH) cofactor. Bilirubin is the major bile, pigment in mammals and has antioxidant and anticompliment activity. We, have determined X-ray crystal structures of apo rat BVR and its complex, with NADH at 1.2 A and 1.5 A resolution, respectively. In agreement with, an independent structure determination of the apo-enzyme, BVR consists of, an N-terminal dinucleotide-binding domain (Rossmann-fold) and a C-terminal, domain that contains a six-stranded beta-sheet that is flanked on one face, by several alpha-helices. The C-terminal and N-terminal domains interact, extensively, forming the active site cleft at their interface. The, cofactor complex structure reported here reveals that the cofactor, nicotinamide ring extends into the active site cleft, where it is adjacent, to conserved amino acid residues and, consistent with the known, stereochemistry of the reaction catalyzed by BVR, the si face of the ring, is accessible for hydride transfer. The only titratable side-chain that, appears to be suitably positioned to function as a general acid in, catalysis is Tyr97. This residue, however, is not essential for catalysis, since the Tyr97Phe mutant protein retains 50% activity. This finding, suggests that the dominant role in catalysis may be performed by hydride, transfer from the cofactor, a process that may be promoted by proximity of, the invariant residues Glu96, Glu123, and Glu126, to the nicotinamide, ring.
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<StructureSection load='1lc0' size='340' side='right'caption='[[1lc0]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1lc0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LC0 FirstGlance]. <br>
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1LC0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Biliverdin_reductase Biliverdin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.24 1.3.1.24] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LC0 OCA].
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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]] 1.2&#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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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==Reference==
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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=1lc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lc0 OCA], [https://pdbe.org/1lc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1lc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lc0 ProSAT]</span></td></tr>
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Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex., Whitby FG, Phillips JD, Hill CP, McCoubrey W, Maines MD, J Mol Biol. 2002 Jun 21;319(5):1199-210. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12079357 12079357]
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</table>
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[[Category: Biliverdin reductase]]
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== Function ==
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[https://www.uniprot.org/uniprot/BIEA_RAT BIEA_RAT] Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.
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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/lc/1lc0_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=1lc0 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Hill CP]]
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[[Category: Hill, C.P.]]
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[[Category: Maines MD]]
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[[Category: Maines, M.D.]]
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[[Category: McCoubrey W]]
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[[Category: McCoubrey, W.]]
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[[Category: Phillips JD]]
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[[Category: Phillips, J.D.]]
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[[Category: Whitby FG]]
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[[Category: Whitby, F.G.]]
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[[Category: PO4]]
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[[Category: bile pigment]]
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[[Category: bilirubin]]
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[[Category: biliverdin reductase]]
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[[Category: heme]]
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[[Category: nadh]]
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[[Category: oxidoreductase]]
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[[Category: tetrapyrrole]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:27:47 2007''
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Current revision

Structure of Biliverdin Reductase and the Enzyme-NADH Complex

PDB ID 1lc0

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