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<StructureSection load='3aw5' size='340' side='right'caption='[[3aw5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3aw5' size='340' side='right'caption='[[3aw5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3aw5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrae Pyrae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AW5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3aw5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._IM2 Pyrobaculum aerophilum str. IM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AW5 FirstGlance]. <br>
</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=C2O:CU-O-CU+LINKAGE'>C2O</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]] 2&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Laccase Laccase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span></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=C2O:CU-O-CU+LINKAGE'>C2O</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=3aw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aw5 OCA], [https://pdbe.org/3aw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aw5 RCSB], [https://www.ebi.ac.uk/pdbsum/3aw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aw5 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=3aw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aw5 OCA], [https://pdbe.org/3aw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aw5 RCSB], [https://www.ebi.ac.uk/pdbsum/3aw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aw5 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8ZWA8_PYRAE Q8ZWA8_PYRAE]
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3aw5" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Laccase 3D structures|Laccase 3D structures]]
*[[Laccase 3D structures|Laccase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Laccase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pyrae]]
[[Category: Pyrobaculum aerophilum str. IM2]]
[[Category: Ohshima, T]]
[[Category: Ohshima T]]
[[Category: Sakuraba, H]]
[[Category: Sakuraba H]]
[[Category: Yoneda, K]]
[[Category: Yoneda K]]
[[Category: Beta barrel]]
[[Category: Oxidoreductase]]

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