2FXT

Crystal Structure of Yeast Tim44

Summary for 2FXT

• Entry DOI: 10.2210/pdb2fxt/pdb
• Descriptor: Import inner membrane translocase subunit TIM44 (1 entity in total)
• Functional Keywords: mitochondrial translocase, protein transport
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Mitochondrion inner membrane ; Peripheral membrane protein : Q01852
• Total number of polymer chains: 1
• Total formula weight: 22018.16

Authors

Josyula, R.,Sha, B. (deposition date: 2006-02-06, release date: 2007-02-06, Last modification date: 2024-02-14)

Primary citation

Josyula, R.,Jin, Z.,Fu, Z.,Sha, B.
Crystal Structure of Yeast Mitochondrial Peripheral Membrane Protein Tim44p C-terminal Domain.
J.Mol.Biol., 359:798-804, 2006

PubMed Abstract: The protein transports from the cell cytosol to the mitochondria matrix are carried out by the translocase of the outer membrane (TOM) complex and the translocase of the inner membrane (TIM) complexes. Tim44p is an essential mitochondrial peripheral membrane protein and a major component of TIM23 translocon. Tim44p can tightly associate with the inner mitochondrial membrane. To investigate the mechanism by which Tim44p functions in the TIM23 translocon to deliver the mitochondrial protein precursors, we have determined the crystal structure of the yeast Tim44p C-terminal domain to 3.2A resolution using the MAD method. The Tim44p C-terminal domain forms a monomer in the crystal structure and contains six alpha-helices and four antiparallel beta-strands. A large hydrophobic pocket was identified on the Tim44p structure surface. The N-terminal helix A1 is positively charged and the helix A1 protrudes out from the Tim44p main body.

PubMed: 16647716
DOI: 10.1016/j.jmb.2006.04.020

Experimental method

X-RAY DIFFRACTION (3.2 Å)