3aw5: Difference between revisions
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==Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum== | ==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=''> | <StructureSection load='3aw5' size='340' side='right'caption='[[3aw5]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3aw5]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AW5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3aw5]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AW5 FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Laccase]] | [[Category: Laccase]] | ||
[[Category: Large Structures]] | |||
[[Category: Pyrae]] | [[Category: Pyrae]] | ||
[[Category: Ohshima, T]] | [[Category: Ohshima, T]] | ||
Revision as of 10:20, 31 July 2019
Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilumStructure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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