3QLE

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

Summary for 3QLE

• Entry DOI: 10.2210/pdb3qle/pdb
• Descriptor: Tim50p, CALCIUM ION, ACETATE ION, ... (5 entities in total)
• Functional Keywords: chaperone, mitochondrion, preprotein translocation
• Biological source: Saccharomyces cerevisiae EC1118 (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 24266.70

Authors

Qian, X.G.,Gebert, M.,Hpker, J.,Yan, M.,Li, J.Z.,Wiedemann, N.,Laan, M.V.D.,Pfanner, N.,Sha, B.D. (deposition date: 2011-02-02, release date: 2011-03-02, Last modification date: 2023-09-13)

Primary citation

Qian, X.,Gebert, M.,Hopker, J.,Yan, M.,Li, J.,Wiedemann, N.,van der Laan, M.,Pfanner, N.,Sha, B.
Structural basis for the function of tim50 in the mitochondrial presequence translocase.
J.Mol.Biol., 411:513-519, 2011

PubMed 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.

PubMed: 21704637
DOI: 10.1016/j.jmb.2011.06.020

Experimental method

X-RAY DIFFRACTION (1.831 Å)