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

Authors :
Qian, Xinguo
Gebert, Michael
Höpker, Jan
Yan, Ming
Li, Jingzhi
Wiedemann, Nils
van der Laan, Martin
Pfanner, Nikolaus
Sha, Bingdong
Source :
Journal of Molecular Biology. Aug2011, Vol. 411 Issue 3, p513-519. 7p.
Publication Year :
2011

Abstract

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. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
00222836
Volume :
411
Issue :
3
Database :
Academic Search Index
Journal :
Journal of Molecular Biology
Publication Type :
Academic Journal
Accession number :
63555338
Full Text :
https://doi.org/10.1016/j.jmb.2011.06.020