View source for 5ys5


==Crystal structure of Multicopper Oxidase CueO G304K mutant with seven copper ions==
<StructureSection load='5ys5' size='340' side='right'caption='[[5ys5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ys5]] 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=5YS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YS5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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></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=5ys5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ys5 OCA], [https://pdbe.org/5ys5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ys5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ys5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ys5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CUEO_ECOLI CUEO_ECOLI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The multicopper oxidase CueO is involved in copper homeostasis and copper (Cu) tolerance in Escherichia coli. The laccase activity of CueO G304K mutant is higher than wild-type CueO. To explain this increase in activity, we solved the crystal structure of G304K mutant at 1.49 A. Compared with wild-type CueO, the G304K mutant showed dramatic conformational changes in methionine-rich helix and the relative regulatory loop (R-loop). We further solved the structure of Cu-soaked enzyme, and found that the addition of Cu ions induced further conformational changes in the R-loop and methionine-rich helix as a result of the new Cu-binding sites on the enzyme's surface. We propose a mechanism for the enhanced laccase activity of the G304K mutant, where movements of the R-loop combined with the changes of the methionine-rich region uncover the T1 Cu site allowing greater access of the substrate. Two of the G304K double mutants showed the enhanced or decreased laccase activity, providing further evidence for the interaction between the R-loop and the methionine-rich region. The cuprous oxidase activity of these mutants was about 20% that of wild-type CueO. These structural features of the G304K mutant provide clues for designing specific substrate-binding mutants in the biotechnological applications.

Crystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity.,Wang H, Liu X, Zhao J, Yue Q, Yan Y, Gao Z, Dong Y, Zhang Z, Fan Y, Tian J, Wu N, Gong Y Sci Rep. 2018 Sep 24;8(1):14252. doi: 10.1038/s41598-018-32446-7. PMID:30250139<ref>PMID:30250139</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ys5" style="background-color:#fffaf0;"></div>

==See Also==
*[[Blue copper oxidase CueO 3D structures|Blue copper oxidase CueO 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Dong YH]]
[[Category: Fan YL]]
[[Category: Gong Y]]
[[Category: Liu XQ]]
[[Category: Tian J]]
[[Category: Wang HQ]]
[[Category: Wu NF]]
[[Category: Yan YH]]
[[Category: Yue QX]]
[[Category: Zhao JT]]