3AW5

Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum

Summary for 3AW5

• Entry DOI: 10.2210/pdb3aw5/pdb
• Descriptor: Multicopper oxidase, COPPER (II) ION, CU-O-CU LINKAGE, ... (5 entities in total)
• Functional Keywords: beta barrel, oxidoreductase
• Biological source: Pyrobaculum aerophilum
• Total number of polymer chains: 1
• Total formula weight: 50049.17

Authors

Sakuraba, H.,Ohshima, T.,Yoneda, K. (deposition date: 2011-03-10, release date: 2011-06-08, Last modification date: 2024-03-13)

Primary citation

Sakuraba, H.,Koga, K.,Yoneda, K.,Kashima, Y.,Ohshima, T.
Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum
Acta Crystallogr.,Sect.F, 67:753-757, 2011

PubMed Abstract: 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 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 α-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.

PubMed: 21795787
DOI: 10.1107/S1744309111018173

Experimental method

X-RAY DIFFRACTION (2 Å)