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Proteins. 2014 Sep;82(9):2263-7. doi: 10.1002/prot.24535. Epub 2014 Mar 20.

Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily.

Author information

1
Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois, 60208.

Abstract

The ammonia monooxygenase (AMO)/particulate methane monooxygenase (pMMO) superfamily is a diverse group of membrane-bound enzymes of which only pMMO has been characterized on the molecular level. The pMMO active site is believed to reside in the soluble N-terminal region of the pmoB subunit. To understand the degree of structural conservation within this superfamily, the crystal structure of the corresponding domain of an archaeal amoB subunit from Nitrosocaldus yellowstonii has been determined to 1.8 Å resolution. The structure reveals a remarkable conservation of overall fold and copper binding site location as well as several notable differences that may have implications for function and stability.

KEYWORDS:

AMO; amoB; copper; crystal structure; cupredoxin; hydrocarbon monooxygenase; methanotroph; pMMO

PMID:
24523098
PMCID:
PMC4133332
DOI:
10.1002/prot.24535
[Indexed for MEDLINE]
Free PMC Article

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