Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 359, Issue 3, Pages 798-804Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.04.020
Keywords
mitochondrion; Tim44; crystal structure; membrane protein
Categories
Funding
- NIDDK NIH HHS [R01 DK56203] Funding Source: Medline
- NIGMS NIH HHS [R01 GM65959, R01 GM080261] Funding Source: Medline
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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 3.2 angstrom 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. (c) 2006 Elsevier Ltd. All rights reserved.
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