5zd6: Difference between revisions
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The | ==High resolution structure of bilirubin oxidase from Myrothecium verrucaria - wild type== | ||
<StructureSection load='5zd6' size='340' side='right' caption='[[5zd6]], [[Resolution|resolution]] 1.46Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5zd6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZD6 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bilirubin_oxidase Bilirubin oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.5 1.3.3.5] </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=5zd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zd6 OCA], [http://pdbe.org/5zd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zd6 RCSB], [http://www.ebi.ac.uk/pdbsum/5zd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zd6 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bilirubin oxidase (BOD) belongs to the family of blue multicopper oxidases, and catalyzes the concomitant oxidation of bilirubin to biliverdin and the reduction of molecular oxygen to water via a four-electron reduction system. The active sites of BOD comprise four copper atoms; type I copper (T1Cu) forms a mononuclear site, and a cluster of three copper atoms forms a trinuclear center. In the present study, we determined the high-resolution crystal structures of BOD from the fungus Myrothecium verrucaria. We investigated wild-type (WT) BOD and a BOD mutant called Met467Gln, which is inactive against bilirubin. The structures revealed that a novel post-translational crosslink between Trp396 and His398 is formed in the vicinity of the T1Cu site in WT, whereas it is absent in the Met467Gln mutant. Our structural, computational, and electrochemical studies suggest that the His-Trp crosslink adjusts the redox potential of T1Cu to that of bilirubin to efficiently abstract electrons from the substrate. | |||
Redox potential-dependent formation of an unusual His-Trp bond in bilirubin oxidase.,Akter M, Tokiwa T, Shoji M, Nishikawa K, Shigeta Y, Sakurai T, Higuchi Y, Kataoka K, Shibata N Chemistry. 2018 Aug 29. doi: 10.1002/chem.201803798. PMID:30156345<ref>PMID:30156345</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5zd6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bilirubin oxidase]] | |||
[[Category: Akter, M]] | |||
[[Category: Higuchi, Y]] | |||
[[Category: Shibata, N]] | |||
[[Category: Multicopper oxydase]] | |||
[[Category: Oxidoreductase]] | |||
Latest revision as of 22:41, 19 September 2018
High resolution structure of bilirubin oxidase from Myrothecium verrucaria - wild typeHigh resolution structure of bilirubin oxidase from Myrothecium verrucaria - wild type
Structural highlights
Publication Abstract from PubMedBilirubin oxidase (BOD) belongs to the family of blue multicopper oxidases, and catalyzes the concomitant oxidation of bilirubin to biliverdin and the reduction of molecular oxygen to water via a four-electron reduction system. The active sites of BOD comprise four copper atoms; type I copper (T1Cu) forms a mononuclear site, and a cluster of three copper atoms forms a trinuclear center. In the present study, we determined the high-resolution crystal structures of BOD from the fungus Myrothecium verrucaria. We investigated wild-type (WT) BOD and a BOD mutant called Met467Gln, which is inactive against bilirubin. The structures revealed that a novel post-translational crosslink between Trp396 and His398 is formed in the vicinity of the T1Cu site in WT, whereas it is absent in the Met467Gln mutant. Our structural, computational, and electrochemical studies suggest that the His-Trp crosslink adjusts the redox potential of T1Cu to that of bilirubin to efficiently abstract electrons from the substrate. Redox potential-dependent formation of an unusual His-Trp bond in bilirubin oxidase.,Akter M, Tokiwa T, Shoji M, Nishikawa K, Shigeta Y, Sakurai T, Higuchi Y, Kataoka K, Shibata N Chemistry. 2018 Aug 29. doi: 10.1002/chem.201803798. PMID:30156345[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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