𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The crystallographic structure of subunit E from Pyrococcus horikoshii OT3 A-ATP synthase reveals the flexibility of the peripheral stalk

✍ Scribed by Balakrishna, A.M.; Grüber, G.

Book ID
123245122
Publisher
Elsevier Science
Year
2012
Tongue
English
Weight
86 KB
Volume
1817
Category
Article
ISSN
0005-2728

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Structure of the catalytic nucleotide-bi
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