2KK7

NMR solution structure of the N terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii

2KK7 の概要

• エントリーDOI: 10.2210/pdb2kk7/pdb
• NMR情報: BMRB: 16354
• 分子名称: V-type ATP synthase subunit E (1 entity in total)
• 機能のキーワード: subunit e, methanocaldococcus jannaschii, a1ao atp synthase, atp synthesis, hydrogen ion transport, ion transport, transport, hydrolase
• 由来する生物種: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5767.81

構造登録者

Gayen, S.,Balakrishna, A.,Gruber, G. (登録日: 2009-06-16, 公開日: 2009-07-14, 最終更新日: 2024-05-29)

主引用文献

Gayen, S.,Balakrishna, A.M.,Gruber, G.
NMR solution structure of the N-terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii
J.Bioenerg.Biomembr., 41:343-348, 2009

PubMed Abstract: The N-termini of E and H of A1AO ATP synthase have been shown to interact and an NMR structure of N-terminal H1-47 has been solved recently. In order to understand the E-H assembly and the N-terminal structure of E, the truncated construct E1-52 of Methanocaldococcus jannaschii A1AO ATP synthase was produced, purified and the solution structure of E1-52 was determined by NMR spectroscopy. The protein is 60.5 A in length and forms an alpha helix between the residues 8-48. The molecule is amphipathic with a strip of hydrophobic residues, discussed as a possible helix-helix interaction with neighboring subunit H.

PubMed: 19760172
DOI: 10.1007/s10863-009-9237-3

実験手法

SOLUTION NMR