Crystal structure of the mitochondrial chaperone TIM9 center dot 10 reveals a six-bladed alpha-propeller
Details
Publication Year 2006-01-06, Volume 21, Issue #1, Page 123-133
Journal Title
MOLECULAR CELL
Publication Type
Journal Article
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 circle 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 circle 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 circle 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 circle 10 as surrogate lipid contacts. The first reported crystal structure of a mitochondrial translocase assembly provides insights into selectivity and regulation of precursor import.
Publisher
CELL PRESS
Keywords
ADP ATP CARRIER; INTERMEMBRANE SPACE; ADP/ATP CARRIER; PROTEIN IMPORT; IN-VIVO; TRANSLOCATION; COMPLEX; MEMBRANES; TIM10; OUTER
Rights Notice
Refer to copyright notice on published article.


Creation Date: 2006-01-06 12:00:00
Last Modified: 0001-01-01 12:00:00
An error has occurred. This application may no longer respond until reloaded. Reload 🗙