2BSK

Crystal structure of the TIM9 Tim10 hexameric complex

2BSK の概要

• エントリーDOI: 10.2210/pdb2bsk/pdb
• 分子名称: MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM9 A, MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM10 (2 entities in total)
• 機能のキーワード: protein transport, tim9, tim10, mitochondrial protein import, tim complex
• 由来する生物種: HOMO SAPIENS; 詳細
• 細胞内の位置: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side: Q9Y5J7 P62072
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 63348.20

構造登録者

Webb, C.T.,Gorman, M.A.,Lazarus, M.,Ryan, M.T.,Gulbis, J.M. (登録日: 2005-05-23, 公開日: 2006-01-04, 最終更新日: 2024-11-20)

主引用文献

Webb, C.T.,Gorman, M.A.,Lazarou, M.,Ryan, M.T.,Gulbis, J.M.
Crystal Structure of the Mitochondrial Chaperone Tim910 Reveals a Six-Bladed Alpha-Propeller.
Mol.Cell, 21:123-, 2006

PubMed Abstract: Import of proteins into mitochondria occurs by coordinated actions of preprotein translocases in the outer and inner membranes. Tim9 and Tim10 are translocase components of the intermembrane space, related to deafness-dystonia peptide 1 (DDP1). They coassemble into a hexamer, TIM9.10, which captures and chaperones precursors of inner membrane metabolite carriers as they exit the TOM channel in the outer membrane. The crystal structure of TIM9.10 reveals a previously undescribed alpha-propeller topology in which helical "blades" radiate from a narrow central pore lined with polar residues. The propeller blades are reminiscent of "tentacles" in chaperones Skp and prefoldin. In each TIM9.10 subunit, a signature "twin CX3C" motif forms two intramolecular disulfides. There is no obvious binding pocket for precursors, which we suggest employ the chaperone-like tentacles of TIM9.10 as surrogate lipid contacts. The first reported crystal structure of a mitochondrial translocase assembly provides insights into selectivity and regulation of precursor import.

PubMed: 16387659
DOI: 10.1016/J.MOLCEL.2005.11.010

実験手法

X-RAY DIFFRACTION (3.3 Å)