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Tim9-Tim10 complex
Tim9 and Tim10 make up the group of essential small Tim proteins that assist in transport of hydrophobic precursors across the intermembrane space. Both Tim9 and Tim10 form a hexamer, the Tim9-Tim10 complex, that when associated, functions as a chaperone to assist translocation of preproteins from the outer mitochondrial membrane to the translocase of the inner membrane. The functional Tim9-Tim10 complex not only directs preproteins to the inner mitochondrial membrane in order to interact with the TIM22 complex, but also guides β-barrel precursor proteins to the sorting and assembly machinery (SAM) of the outer membrane.
==Structure of the Tim9-Tim10 complex==
The Tim9-Tim10 complex is made up of three Tim9 molecules and three Tim10 molecules. Each Tim9 and Tim10 subunit consists of 80-110 amino acid residues with four conserved cysteine residues that form two intramolecular disulfide bonds.〔Webb, C.T., Gorman, M.A., Lazarou, M., Ryan, M.T., Gulbis, J.M. (2006) Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller. Mol. Cell. 21(1): 123-133.〕 Each subunit folds into a helix-loop-helix structure, with each loop forming a donut shape that comprises the upper face of the complex. The structure of the Tim9-Tim10 complex takes on the form of an α-propeller, with two helical blades radiating from a narrow central pore.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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