2BSK

Crystal structure of the TIM9 Tim10 hexameric complex

Summary for 2BSK

• Entry DOI: 10.2210/pdb2bsk/pdb
• Descriptor: MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM9 A, MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM10 (2 entities in total)
• Functional Keywords: protein transport, tim9, tim10, mitochondrial protein import, tim complex
• Biological source: HOMO SAPIENS; More
• Cellular location: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side: Q9Y5J7 P62072
• Total number of polymer chains: 6
• Total formula weight: 63348.20

Authors

Webb, C.T.,Gorman, M.A.,Lazarus, M.,Ryan, M.T.,Gulbis, J.M. (deposition date: 2005-05-23, release date: 2006-01-04, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.3 Å)