1he3: Difference between revisions
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==Human biliverdin IX beta reductase: NADP/mesobiliverdin IV alpha ternary complex== | |||
<StructureSection load='1he3' size='340' side='right' caption='[[1he3]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='1he3' size='340' side='right' caption='[[1he3]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hdo|1hdo]], [[1he2|1he2]], [[1he4|1he4]], [[1he5|1he5]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hdo|1hdo]], [[1he2|1he2]], [[1he4|1he4]], [[1he5|1he5]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1he3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1he3 OCA], [http://pdbe.org/1he3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1he3 RCSB], [http://www.ebi.ac.uk/pdbsum/1he3 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1he3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1he3 OCA], [http://pdbe.org/1he3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1he3 RCSB], [http://www.ebi.ac.uk/pdbsum/1he3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1he3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/he/1he3_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/he/1he3_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1he3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1he3" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:29, 10 January 2018
Human biliverdin IX beta reductase: NADP/mesobiliverdin IV alpha ternary complexHuman biliverdin IX beta reductase: NADP/mesobiliverdin IV alpha ternary complex
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBiliverdin IXbeta reductase (BVR-B) catalyzes the pyridine nucleotide-dependent production of bilirubin-IXbeta, the major heme catabolite during early fetal development. BVR-B displays a preference for biliverdin isomers without propionates straddling the C10 position, in contrast to biliverdin IXalpha reductase (BVR-A), the major form of BVR in adult human liver. In addition to its tetrapyrrole clearance role in the fetus, BVR-B has flavin and ferric reductase activities in the adult. We have solved the structure of human BVR-B in complex with NADP+ at 1.15 A resolution. Human BVR-B is a monomer displaying an alpha/beta dinucleotide binding fold. The structures of ternary complexes with mesobiliverdin IValpha, biliverdin IXalpha, FMN and lumichrome show that human BVR-B has a single substrate binding site, to which substrates and inhibitors bind primarily through hydrophobic interactions, explaining its broad specificity. The reducible atom of both biliverdin and flavin substrates lies above the reactive C4 of the cofactor, an appropriate position for direct hydride transfer. BVR-B discriminates against the biliverdin IXalpha isomer through steric hindrance at the bilatriene side chain binding pockets. The structure also explains the enzyme's preference for NADP(H) and its B-face stereospecificity. Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme.,Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M Nat Struct Biol. 2001 Mar;8(3):215-20. PMID:11224564[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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