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Crystallization and preliminary X-ray analysis of mitochondrial presequence receptor Tom20 in complexes with a presequence from aldehyde dehydrogenase.

Authors: Igura, Mayumi  Ose, Toyoyuki  Obita, Takayuki  Sato, Chiaki  Maenaka, Katsumi  Endo, Toshiya  Kohda, Daisuke 
Citation: Igura M, etal., Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt 5):514-7. doi: 10.1107/S1744309105011577. Epub 2005 Apr 22.
Pubmed: (View Article at PubMed) PMID:16511083
DOI: Full-text: DOI:10.1107/S1744309105011577

Most mitochondrial proteins are synthesized in the cytosol and must be imported into the mitochondria. Many mitochondrial precursor proteins have an extra leader sequence at their N-terminus called a presequence. Presequences are recognized by the Tom20 receptor protein. Based on the previously determined NMR structure of rat Tom20, a fragment corresponding to the core structure was generated. A cysteine residue was added at the C-terminus of the rat aldehyde dehydrogenase presequence to fix the presequence peptide onto the Tom20 fragment via an intermolecular disulfide bond. Two crystal forms of the complex were successfully obtained with different designs of the linker sequence which diffracted to 2.1 and 1.9 A. Crystal dehydration and subsequent annealing was essential to obtain good diffraction data for the 2.1 A crystal form.


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RGD ID: 13463599
Created: 2017-12-20
Species: All species
Last Modified: 2017-12-20
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.