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ABSTRACT:
SUBMITTER: Sakuraba H
PROVIDER: S-EPMC3144789 | biostudies-literature | 2011 Jul
REPOSITORIES: biostudies-literature
Sakuraba Haruhiko H Koga Kohtaroh K Yoneda Kazunari K Kashima Yasuhiro Y Ohshima Toshihisa T
Acta crystallographica. Section F, Structural biology and crystallization communications 20110624 Pt 7
The crystal structure of an extremely thermostable multicopper oxidase (McoP) from the hyperthermophilic archaeon Pyrobaculum aerophilum was determined at a resolution of 2.0 Å. 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 ...[more]