Crystallization and preliminary X-ray analysis of mitochondrial presequence receptor Tom20 in complexes with a presequence from aldehyde dehydrogenase
Journal Article
·
· Acta Crystallographica. Section F
- Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582 (Japan)
- Department of Structural Biology, Bioengineering Research Institute, Furuedai, Osaka 565-0874 (Japan)
- Department of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602 (Japan)
A presequence peptide derived from rat aldehyde dehydrogenase was tethered to the cytosolic domain of rat Tom20 protein via an intermolecular disulfide bond. Two crystal forms were obtained with different linker designs and diffracted to 2.1 and 1.9 Å. 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 Å. Crystal dehydration and subsequent annealing was essential to obtain good diffraction data for the 2.1 Å crystal form.
- OSTI ID:
- 22356004
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 5 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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