2K6I

The domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H1-47

2K6I の概要

• エントリーDOI: 10.2210/pdb2k6i/pdb
• NMR情報: BMRB: 15870
• 分子名称: Uncharacterized protein MJ0223 (1 entity in total)
• 機能のキーワード: h subunit, a1ao atp synthase, v1vo atpase, f1fo atp synthase, methanocaldococcus jannaschii, structural protein
• 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: 6394.44

構造登録者

Biukovic, N.,Gayen, S.,Pervushin, K.,Gruber, G.,Biukovic, G. (登録日: 2008-07-09, 公開日: 2009-07-21, 最終更新日: 2024-05-08)

主引用文献

Biukovic, G.,Gayen, S.,Pervushin, K.,Gruber, G.
Domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H(1-47).
Biophys.J., 97:286-294, 2009

PubMed Abstract: A series of truncated forms of subunit H were generated to establish the domain features of that protein. Circular dichroism analysis demonstrated that H is divided at least into a C-terminal coiled-coil domain within residues 54-104, and an N-terminal domain formed by adjacent alpha-helices. With a cysteine at the C-terminus of each of the truncated proteins (H(1-47), H(1-54), H(1-59), H(1-61), H(1-67), H(1-69), H(1-71), H(1-78), H(1-80), H(1-91), and H(47-105)), the residues involved in formation of the coiled-coil interface were determined. Proteins H(1-54), H(1-61), H(1-69), and H(1-80) showed strong cross-link formation, which was weaker in H(1-47), H(1-59), H(1-71), and H(1-91). A shift in disulfide formation between cysteines at positions 71 and 80 reflected an interruption in the periodicity of hydrophobic residues in the region 71AEKILEETEKE81. To understand how the N-terminal domain of H is formed, we determined for the first time, to our knowledge, the solution NMR structure of H(1-47), which revealed an alpha-helix between residues 15-42 and a flexible N-terminal stretch. The alpha-helix includes a kink that would bring the two helices of the C-terminus into the coiled-coil arrangement. H(1-47) revealed a strip of alanines involved in dimerization, which were tested by exchange to single cysteines in subunit H mutants.

PubMed: 19580766
DOI: 10.1016/j.bpj.2009.04.026

実験手法

SOLUTION NMR