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| | <StructureSection load='4ner' size='340' side='right'caption='[[4ner]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='4ner' size='340' side='right'caption='[[4ner]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ner]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4e9p 4e9p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NER FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ner]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4e9p 4e9p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NER 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=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e9q|4e9q]], [[4e9r|4e9r]], [[4e9s|4e9s]], [[4e9t|4e9t]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cueO, yacK, b0123, JW0119 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ner FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ner OCA], [https://pdbe.org/4ner PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ner RCSB], [https://www.ebi.ac.uk/pdbsum/4ner PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ner ProSAT]</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=4ner FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ner OCA], [http://pdbe.org/4ner PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ner RCSB], [http://www.ebi.ac.uk/pdbsum/4ner PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ner ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/CUEO_ECOLI CUEO_ECOLI] |
| - | Structural models determined by X-ray crystallography play a central role in understanding the catalytic mechanism of enzymes. However, X-ray radiation generates hydrated electrons that can cause significant damage to the active sites of metalloenzymes. In the present study, crystal structures of the multicopper oxidases (MCOs) CueO from Escherichia coli and laccase from a metagenome were determined. Diffraction data were obtained from a single crystal under low to high X-ray dose conditions. At low levels of X-ray exposure, unambiguous electron density for an O atom was observed inside the trinuclear copper centre (TNC) in both MCOs. The gradual reduction of copper by hydrated electrons monitored by measurement of the Cu K-edge X-ray absorption spectra led to the disappearance of the electron density for the O atom. In addition, the size of the copper triangle was enlarged by a two-step shift in the location of the type III coppers owing to reduction. Further, binding of O2 to the TNC after its full reduction was observed in the case of the laccase. Based on these novel structural findings, the diverse resting structures of the MCOs and their four-electron O2-reduction process are discussed.
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| - | New insights into the catalytic active-site structure of multicopper oxidases.,Komori H, Sugiyama R, Kataoka K, Miyazaki K, Higuchi Y, Sakurai T Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):772-9. doi:, 10.1107/S1399004713033051. Epub 2014 Feb 22. PMID:24598746<ref>PMID:24598746</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 4ner" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Blue copper oxidase CueO 3D structures|Blue copper oxidase CueO 3D structures]] | | *[[Blue copper oxidase CueO 3D structures|Blue copper oxidase CueO 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Higuchi, Y]] | + | [[Category: Higuchi Y]] |
| - | [[Category: Kataoka, K]] | + | [[Category: Kataoka K]] |
| - | [[Category: Komori, H]] | + | [[Category: Komori H]] |
| - | [[Category: Sakurai, T]] | + | [[Category: Sakurai T]] |
| - | [[Category: Oxidoreductase]]
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