2guz
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(New page: 200px<br /><applet load="2guz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2guz, resolution 2.00Å" /> '''Structure of the Tim...)
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Revision as of 09:17, 21 November 2007
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Structure of the Tim14-Tim16 complex of the mitochondrial protein import motor
Overview
The import motor of the mitochondrial translocase of the inner membrane, (TIM23) mediates the ATP-dependent translocation of preproteins into the, mitochondrial matrix by cycles of binding to and release from mtHsp70. An, essential step of this process is the stimulation of the ATPase activity, of mtHsp70 performed by the J cochaperone Tim14. Tim14 forms a complex, with the J-like protein Tim16. The crystal structure of this complex shows, that the conserved domains of the two proteins have virtually identical, folds but completely different surfaces enabling them to perform different, functions. The Tim14-Tim16 dimer reveals a previously undescribed, arrangement of J and J-like domains. Mutations that destroy the complex, between Tim14 and Tim16 are lethal demonstrating that complex formation is, an essential requirement for the viability of cells. We further, demonstrate tight regulation of the cochaperone activity of Tim14 by, Tim16. The first crystal structure of a J domain in complex with a, regulatory protein provides new insights into the function of the, mitochondrial TIM23 translocase and the Hsp70 chaperone system in general.
About this Structure
2GUZ is a Protein complex structure of sequences from Saccharomyces cerevisiae with FLC as ligand. Full crystallographic information is available from OCA.
Reference
Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor., Mokranjac D, Bourenkov G, Hell K, Neupert W, Groll M, EMBO J. 2006 Oct 4;25(19):4675-85. Epub 2006 Sep 14. PMID:16977310
Page seeded by OCA on Wed Nov 21 11:24:18 2007
