1HF9

C-Terminal Coiled-Coil Domain from Bovine IF1

1HF9 の概要

• エントリーDOI: 10.2210/pdb1hf9/pdb
• NMR情報: BMRB: 4906
• 分子名称: ATPASE INHIBITOR (MITOCHONDRIAL) (1 entity in total)
• 機能のキーワード: atpase inhibitor, f1 atpase inhibitor, mitochondrion, transit peptide
• 由来する生物種: BOS TAURUS (COW)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 9999.23

構造登録者

Gordon-Smith, D.J.,Carbajo, R.J.,Yang, J.-C.,Videler, H.,Runswick, M.J.,Walker, J.E.,Neuhaus, D. (登録日: 2000-11-30, 公開日: 2001-05-31, 最終更新日: 2024-05-15)

主引用文献

Gordon-Smith, D.J.,Carbajo, R.J.,Yang, J.C.,Videler, H.,Runswick, M.J.,Walker, J.E.,Neuhaus, D.
Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.
J. Mol. Biol., 308:325-339, 2001

PubMed Abstract: Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface.

PubMed: 11327770
DOI: 10.1006/jmbi.2001.4570

実験手法

SOLUTION NMR