2fqe
From Proteopedia
(Difference between revisions)
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<StructureSection load='2fqe' size='340' side='right'caption='[[2fqe]], [[Resolution|resolution]] 1.92Å' scene=''> | <StructureSection load='2fqe' size='340' side='right'caption='[[2fqe]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2fqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2fqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FQE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2O:CU-O-CU+LINKAGE'>C2O</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2O:CU-O-CU+LINKAGE'>C2O</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=2fqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fqe OCA], [https://pdbe.org/2fqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fqe RCSB], [https://www.ebi.ac.uk/pdbsum/2fqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fqe ProSAT]</span></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=2fqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fqe OCA], [https://pdbe.org/2fqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fqe RCSB], [https://www.ebi.ac.uk/pdbsum/2fqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fqe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CUEO_ECOLI CUEO_ECOLI] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=2fqe ConSurf]. | </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=2fqe ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | CueO protein is a hypothetical bacterial laccase and a good laccase candidate for large scale industrial application. Four CueO crystal structures were determined at different copper concentrations. Low copper occupancy in apo-CueO and slow copper reconstitution process in CueO with exogenous copper were demonstrated. These observations well explain the copper dependence of CueO oxidase activity. Structural comparison between CueO and other three fungal laccase proteins indicates that Glu106 in CueO constitutes the primary counter-work for reconstitution of the trinuclear copper site. Mutation of Glu106 to a Phe enhanced CueO oxidation activity and supported this hypothesis. In addition, an extra alpha-helix from Leu351 to Gly378 covers substrate biding pocket of CueO and might compromises the electron transfer from substrate to type I copper. | ||
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| - | Crystal structures of E. coli laccase CueO at different copper concentrations.,Li X, Wei Z, Zhang M, Peng X, Yu G, Teng M, Gong W Biochem Biophys Res Commun. 2007 Mar 2;354(1):21-6. Epub 2006 Dec 22. PMID:17217912<ref>PMID:17217912</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2fqe" style="background-color:#fffaf0;"></div> | ||
==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: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Gong | + | [[Category: Gong W]] |
| - | [[Category: Li | + | [[Category: Li X]] |
| - | [[Category: Teng | + | [[Category: Teng M]] |
| - | [[Category: Wei | + | [[Category: Wei Z]] |
| - | [[Category: Zhang | + | [[Category: Zhang M]] |
| - | + | ||
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Current revision
Crystal Structures of E. coli Laccase CueO under different copper binding situations
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Categories: Escherichia coli | Large Structures | Gong W | Li X | Teng M | Wei Z | Zhang M
