3aw5: Difference between revisions
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==Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum== | |||
<StructureSection load='3aw5' size='340' side='right'caption='[[3aw5]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8ZWA8_PYRAE Q8ZWA8_PYRAE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3aw5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Laccase 3D structures|Laccase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrobaculum aerophilum str. IM2]] | |||
[[Category: Ohshima T]] | |||
[[Category: Sakuraba H]] | |||
[[Category: Yoneda K]] | |||
Latest revision as of 08:54, 13 August 2026
Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum
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