4e9r

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Current revision (08:49, 20 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e9r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E9R FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e9r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E9R FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=4e9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9r OCA], [https://pdbe.org/4e9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e9r RCSB], [https://www.ebi.ac.uk/pdbsum/4e9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9r 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=4e9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9r OCA], [https://pdbe.org/4e9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e9r RCSB], [https://www.ebi.ac.uk/pdbsum/4e9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CUEO_ECOLI CUEO_ECOLI]]
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[https://www.uniprot.org/uniprot/CUEO_ECOLI CUEO_ECOLI]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CueO is a multicopper oxidase (MCO) that is involved in the homeostasis of Cu in Escherichia coli and is the sole cuprous oxidase to have ever been found. Differing from other MCOs, the substrate-binding site of CueO is deeply buried under a methionine-rich helical region including alpha-helices 5, 6, and 7 that interfere with the access of organic substrates. We deleted the region Pro357-His406 and replaced it with a Gly-Gly linker. The crystal structures of a truncated mutant in the presence and in the absence of excess Cu(II) indicated that the scaffold of the CueO molecule and metal-binding sites were reserved in comparison with those of CueO. In addition, the high thermostability of the protein molecule and its spectroscopic and magnetic properties due to four Cu centers were also conserved after truncation. As for functions, the cuprous oxidase activity of the mutant was reduced to ca 10% that of recombinant CueO owing to the decrease in the affinity of the labile Cu site for Cu(I) ions, although activities for laccase substrates such as 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), p-phenylenediamine, and 2,6-dimethoxyphenol increased due to changes in the access of these organic substrates to the type I Cu site. The present engineering of CueO indicates that the methionine-rich alpha-helices function as a barrier to the access of bulky organic substrates, which provides CueO with specificity as a cuprous oxidase.
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Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site.,Kataoka K, Komori H, Ueki Y, Konno Y, Kamitaka Y, Kurose S, Tsujimura S, Higuchi Y, Kano K, Seo D, Sakurai T J Mol Biol. 2007 Oct 12;373(1):141-52. Epub 2007 Aug 2. PMID:17804014<ref>PMID:17804014</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4e9r" 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]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Multicopper Oxidase CueO (data4)

PDB ID 4e9r

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