The C-terminal aqueous-exposed domain of the 45 kDa subunit of the particulate methane monooxygenase in Methylococcus capsulatus

The analysis of crystal structure of particulate methane monooxygenase (pMMO), membrane-bound metalloenzyme isolated from Methylococcus capsulatus is described. The results reveal that the C-terminal subdomain folds into a [beta]-sheet structure in the presence of Cu(I) which facilitates the function in the turnover of the enzyme.