3aw5: Difference between revisions

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[[Image:3aw5.png|left|200px]]
==Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum==
<StructureSection load='3aw5' size='340' side='right' caption='[[3aw5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3aw5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AW5 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aw5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aw5 RCSB], [http://www.ebi.ac.uk/pdbsum/3aw5 PDBsum]</span></td></tr>
<table>
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== 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.


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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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===Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
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== References ==
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==About this Structure==
[[3aw5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AW5 OCA].
 
==Reference==
<ref group="xtra">PMID:021795787</ref><references group="xtra"/>
[[Category: Laccase]]
[[Category: Laccase]]
[[Category: Pyrobaculum aerophilum]]
[[Category: Pyrobaculum aerophilum]]

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