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

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.

SUBMITTER: Lawton TJ

PROVIDER: S-EPMC4133332 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature

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

Lawton Thomas J TJ Ham Jungwha J Sun Tianlin T Rosenzweig Amy C AC

Proteins 20140320 9

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 ...[more]

PMID: 24523098

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