title: 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.
authors: Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois, 60208.
authors: Thomas J
authors: TJ
authors: Lawton
authors: Jungwha
authors: J
authors: Ham
authors: Tianlin
authors: T
authors: Sun
authors: Amy C
authors: AC
authors: Rosenzweig
mesh_terms: D000595:Amino Acid Sequence; D001400:Azurin / Q000737:chemistry; D001665:Binding Sites; D020134:Catalytic Domain; D003300:Copper / Q000737:chemistry; D019615:Crenarchaeota / Q000201:enzymology*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000648:ultrastructure*; D010105:Oxygenases / Q000648:ultrastructure*; D011485:Protein Binding; D017510:Protein Folding
chemical_list: C050107:cupredoxin; D001400:Azurin; D003300:Copper; D010088:Oxidoreductases; D010105:Oxygenases; C021555:methane monooxygenase; C045582:ammonia monooxygenase
keywords: AMO; amoB; copper; crystal structure; cupredoxin; hydrocarbon monooxygenase; methanotroph; pMMO