Structural highlights
Function
B0LKZ4_9ARCH
Publication Abstract from PubMed
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 A 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. Proteins 2014. (c) 2014 Wiley Periodicals, Inc.
Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily.,Lawton TJ, Ham J, Sun T, Rosenzweig AC Proteins. 2014 Feb 13. doi: 10.1002/prot.24535. PMID:24523098[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lawton TJ, Ham J, Sun T, Rosenzweig AC. Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily. Proteins. 2014 Feb 13. doi: 10.1002/prot.24535. PMID:24523098 doi:http://dx.doi.org/10.1002/prot.24535
