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

Mayumi Igura, Toyoyuki Ose, Takayuki Obita, Chiaki Sato, Katsumi Maenaka, Toshiya Endo, Daisuke Kohda

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    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 1.9Å. Crystal dehydration and subsequent annealing was essential to obtain good diffraction data for the 2.1Å crystal form.

    Original languageEnglish
    Pages (from-to)514-517
    Number of pages4
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Volume61
    Issue number5
    DOIs
    Publication statusPublished - 2005

    All Science Journal Classification (ASJC) codes

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Genetics
    • Condensed Matter Physics

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