Strucutral conservation of the B subunit in the ammonia monooxygenease/particluate methane monooxygenase superfamily

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.