Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily.
Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily.
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DOI：
10.1002/prot.24535
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发表时间：
2014-09
影响因子：
2.9
通讯作者：
Rosenzweig, Amy C.
中科院分区：
文献类型：
--
作者：
Lawton, Thomas J.;Ham, Jungwha;Sun, Tianlin;Rosenzweig, Amy C.
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 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.
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DOI：
10.1007/0-387-30745-1_36
发表时间：
2006-01-01
期刊：
PROKARYOTES: A HANDBOOK ON THE BIOLOGY OF BACTERIA, VOL 5, THIRD EDITION
影响因子：
--
作者：
Koops, Hans-Peter;Purkhold, Ulrike;Wagner, Michael
通讯作者：
Wagner, Michael
影响因子：
64.8
作者：
通讯作者：
--
影响因子：
2.9
作者：
Hakemian, Amanda S.;Kondapalli, Kalyan C.;Rosenzweig, Amy C.
通讯作者：
Rosenzweig, Amy C.
影响因子：
4.4
作者：
Redmond, Molly C.;Valentine, David L.;Sessions, Alex L.
通讯作者：
Sessions, Alex L.
影响因子：
3.3
作者：
Sayavedra-Soto, Luis A.;Hamamura, Natsuko;Arp, Daniel J.
通讯作者：
Arp, Daniel J.