3QLE

Structural Basis for the Function of Tim50 in the Mitochondrial Presequence Translocase

3QLE の概要

• エントリーDOI: 10.2210/pdb3qle/pdb
• 分子名称: Tim50p, CALCIUM ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: chaperone, mitochondrion, preprotein translocation
• 由来する生物種: Saccharomyces cerevisiae EC1118 (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24266.70

構造登録者

Qian, X.G.,Gebert, M.,Hpker, J.,Yan, M.,Li, J.Z.,Wiedemann, N.,Laan, M.V.D.,Pfanner, N.,Sha, B.D. (登録日: 2011-02-02, 公開日: 2011-03-02, 最終更新日: 2023-09-13)

主引用文献

Qian, X.,Gebert, M.,Hopker, J.,Yan, M.,Li, J.,Wiedemann, N.,van der Laan, M.,Pfanner, N.,Sha, B.
Structural basis for the function of tim50 in the mitochondrial presequence translocase.
J.Mol.Biol., 411:513-519, 2011

PubMed Abstract: Many mitochondrial proteins are synthesized as preproteins carrying amino-terminal presequences in the cytosol. The preproteins are imported by the translocase of the outer mitochondrial membrane and the presequence translocase of the inner membrane. Tim50 and Tim23 transfer preproteins through the intermembrane space to the inner membrane. We report the crystal structure of the intermembrane space domain of yeast Tim50 to 1.83 Å resolution. A protruding β-hairpin of Tim50 is crucial for interaction with Tim23, providing a molecular basis for the cooperation of Tim50 and Tim23 in preprotein translocation to the protein-conducting channel of the mitochondrial inner membrane.

PubMed: 21704637
DOI: 10.1016/j.jmb.2011.06.020

実験手法

X-RAY DIFFRACTION (1.831 Å)