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The crystal structure of a novel SAM-dependent methyltransferase PH1915 from Pyrococcus horikoshii

✍ Scribed by Warren Sun; Xiaohui Xu; Marina Pavlova; Aled M. Edwards; Andrzej Joachimiak; Alexei Savchenko; Dinesh Christendat

Book ID
111752630
Publisher
Cold Spring Harbor Laboratory Press
Year
2005
Tongue
English
Weight
338 KB
Volume
14
Category
Article
ISSN
0961-8368

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Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk
✍ Maegawa, Yuki ;Morita, Hazuki ;Iyaguchi, Daisuke ;Yao, Min ;Watanabe, Nobuhisa ; 📂 Article 📅 2006 🏛 International Union of Crystallography 🌐 English ⚖ 751 KB

H(+)-transporting ATP synthase is a multi-subunit enzyme involved in the production of ATP, which is an essential molecule for living organisms as a source of energy. Archaeal A-type ATPase (A-ATPase) is thought to act as a functional ATP synthase in archaea and is thought to have chimeric propertie