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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q8ZWA8_PYRAE Q8ZWA8_PYRAE] | | [https://www.uniprot.org/uniprot/Q8ZWA8_PYRAE Q8ZWA8_PYRAE] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The crystal structure of an extremely thermostable multicopper oxidase (McoP) from the hyperthermophilic archaeon Pyrobaculum aerophilum was determined at a resolution of 2.0 A. The overall fold was comprised of three cupredoxin-like domains and the main-chain coordinates of the enzyme were similar to those of multicopper oxidases from Escherichia coli (CueO) and Bacillus subtilis (CotA). However, there were clear topological differences around domain 3 between McoP and the other two enzymes: a methionine-rich helix in CueO and a protruding helix in CotA were not present in McoP. Instead, a large loop (PL-1) covered the T1 copper centre of McoP and a short alpha-helix in domain 3 extended near the N-terminal end of PL-1. In addition, the sizes of several surface loops in McoP were markedly smaller than the corresponding loops in CueO and CotA. Structural comparison revealed that the presence of extensive hydrophobic interactions and a smaller cavity volume are likely to be the main factors contributing to the hyperthermostability of McoP.
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| Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum.,Sakuraba H, Koga K, Yoneda K, Kashima Y, Ohshima T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt, 7):753-7. Epub 2011 Jun 24. PMID:21795787<ref>PMID:21795787</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3aw5" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Laccase 3D structures|Laccase 3D structures]] | | *[[Laccase 3D structures|Laccase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |