Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller
- PMID: 16387659
- DOI: 10.1016/j.molcel.2005.11.010
Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller
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.
Comment in
-
Chaperoning through the mitochondrial intermembrane space.Mol Cell. 2006 Jan 20;21(2):145-8. doi: 10.1016/j.molcel.2006.01.001. Mol Cell. 2006. PMID: 16427004 Review.
Similar articles
-
Chaperoning through the mitochondrial intermembrane space.Mol Cell. 2006 Jan 20;21(2):145-8. doi: 10.1016/j.molcel.2006.01.001. Mol Cell. 2006. PMID: 16427004 Review.
-
Allosteric and electrostatic protein-protein interactions regulate the assembly of the heterohexameric Tim9-Tim10 complex.J Mol Biol. 2008 Jun 6;379(3):609-16. doi: 10.1016/j.jmb.2008.04.029. Epub 2008 May 6. J Mol Biol. 2008. PMID: 18462749
-
Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space.Biochem J. 2008 Jan 15;409(2):377-87. doi: 10.1042/BJ20070877. Biochem J. 2008. PMID: 17894549
-
Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10.J Biol Chem. 2003 Oct 3;278(40):38505-13. doi: 10.1074/jbc.M306027200. Epub 2003 Jul 25. J Biol Chem. 2003. PMID: 12882976
-
A dynamic machinery for import of mitochondrial precursor proteins.FEBS Lett. 2007 Jun 19;581(15):2802-10. doi: 10.1016/j.febslet.2007.03.004. Epub 2007 Mar 12. FEBS Lett. 2007. PMID: 17376437 Review.
Cited by
-
Mitochondrial Tim9 protects Tim10 from degradation by the protease Yme1.Biosci Rep. 2015 Mar 17;35(3):e00193. doi: 10.1042/BSR20150038. Biosci Rep. 2015. PMID: 26182355 Free PMC article.
-
Mitochondrial protein import: from proteomics to functional mechanisms.Nat Rev Mol Cell Biol. 2010 Sep;11(9):655-67. doi: 10.1038/nrm2959. Nat Rev Mol Cell Biol. 2010. PMID: 20729931 Review.
-
Adenine nucleotide carrier protein dysfunction in human disease.IUBMB Life. 2023 Nov;75(11):911-925. doi: 10.1002/iub.2767. Epub 2023 Jul 14. IUBMB Life. 2023. PMID: 37449547 Free PMC article. Review.
-
Mitochondrial biogenesis and turnover.Cell Calcium. 2008 Jul;44(1):24-35. doi: 10.1016/j.ceca.2007.12.004. Epub 2008 Apr 18. Cell Calcium. 2008. PMID: 18395251 Free PMC article. Review.
-
Folding and biogenesis of mitochondrial small Tim proteins.Int J Mol Sci. 2013 Aug 13;14(8):16685-705. doi: 10.3390/ijms140816685. Int J Mol Sci. 2013. PMID: 23945562 Free PMC article. Review.
Publication types
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous
