期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 411, 期 3, 页码 513-519出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2011.06.020
关键词
mitochondrial inner membrane; preprotein; protein sorting; Saccharomyces cerevisiae; Tim23
资金
- National Institutes of Health [R01 GM65959]
- Army Research Office [51894LS]
- Deutsche Forschungsgemeinschaft, Sonderforschungsbereich [746]
- Excellence Initiative of the German Federal and State Governments [EXC 294 BIOSS, GSC-4]
- Bundesministerium fur Bildung und Forschung
- Landesforschungspreis Baden-Wurttemberg
- Gottfried Wilhelm Leibniz Program
- Fonds der Chemischen Industrie
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 angstrom resolution. A protruding beta-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. (c) 2011 Elsevier Ltd. All rights reserved.
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