5or3
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Aspergillus oryzae catechol oxidase in met/deoxy-form== | |
| + | <StructureSection load='5or3' size='340' side='right' caption='[[5or3]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5or3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OR3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OR3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PER:PEROXIDE+ION'>PER</scene></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=5or3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5or3 OCA], [http://pdbe.org/5or3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5or3 RCSB], [http://www.ebi.ac.uk/pdbsum/5or3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5or3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Coupled binuclear copper (CBC) enzymes have a conserved type 3 copper site that binds molecular oxygen to oxidize various mono- and diphenolic compounds. In this study, we found a new crystal form of catechol oxidase from Aspergillus oryzae (AoCO4) and solved two new structures from two different crystals at 1.8-A and at 2.5-A resolutions. These structures showed different copper site forms (met/deoxy and deoxy) and also differed from the copper site observed in the previously solved structure of AoCO4. We also analysed the electron density maps of all of the 56 CBC enzyme structures available in the protein data bank (PDB) and found that many of the published structures have vague copper sites. Some of the copper sites were then re-refined to find a better fit to the observed electron density. General problems in the refinement of metalloproteins and metal centres are discussed. | ||
| - | + | A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes.,Penttinen L, Rutanen C, Saloheimo M, Kruus K, Rouvinen J, Hakulinen N PLoS One. 2018 May 1;13(5):e0196691. doi: 10.1371/journal.pone.0196691., eCollection 2018. PMID:29715329<ref>PMID:29715329</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5or3" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hakulinen, N]] | ||
[[Category: Penttinen, L]] | [[Category: Penttinen, L]] | ||
| + | [[Category: Rouvinen, J]] | ||
[[Category: Rutanen, C]] | [[Category: Rutanen, C]] | ||
| - | [[Category: | + | [[Category: Catechol oxidase]] |
| + | [[Category: Coupled binuclear copper enzyme]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Polyphenol oxidase]] | ||
| + | [[Category: Type 3 copper center]] | ||
Revision as of 06:08, 9 May 2018
Crystal structure of Aspergillus oryzae catechol oxidase in met/deoxy-form
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