Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 82, Issue 9, Pages 2263-2267Publisher
WILEY-BLACKWELL
DOI: 10.1002/prot.24535
Keywords
AMO; amoB; copper; crystal structure; cupredoxin; hydrocarbon monooxygenase; methanotroph; pMMO
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Funding
- National Institutes of Health [GM070473]
- U.S. DOE [DE-AC02-06CH11357]
- Michigan Economic Development Corporation
- Michigan Technology Tri-Corridor [085P1000817]
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The ammonia monoxygnase (AMO)/particulate methane monoxygenase (pMMO) superfamily is a divense group of membrane-bound enzymes of which only pMMO has been charaterzed on the moecular level. The pMMO active site is believed to reside in the soluble N-terminal region of the promoB subunit. To understand the degree of sturcual conservation ith this superfamily, the crystal structure of the corresponding deomain of an archael aamob subunit form nitrosocolus yelostani has been determind to 1.8 angstrom resolution. The structure reveals a remarkable consrvation of overall fold and copper binding site location as well as serveral notable differences that may have implications for function and stability.
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