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Updated: Jul 14, 2026
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Crystallization and preliminary X-ray analysis of Atg10
Masaya Yamaguti1, Nobuo N Suzuki, Yuko Fujioka
1Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N-12, W-6, Kita-ku, Sapporo 060-0812, Japan.
Summary
Researchers crystallized Saccharomyces cerevisiae Atg10, an enzyme crucial for autophagy. This structural study provides insights into the essential Atg12-Atg5 conjugation process.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Autophagy is a vital cellular process for degrading cytoplasmic components.
- The Atg12-Atg5 conjugate, facilitated by Atg10, is essential for autophagy.
- Understanding Atg10's structure is key to elucidating autophagy mechanisms.
Purpose of the Study:
- To obtain high-quality crystals of Saccharomyces cerevisiae Atg10.
- To determine the crystal structure of Atg10 for functional analysis.
- To provide structural insights into the Atg12-Atg5 conjugation pathway.
Main Methods:
- Microcrystals of Saccharomyces cerevisiae Atg10 were produced using free-interface diffusion.
- Large crystals suitable for diffraction studies were obtained via sitting-drop vapor diffusion.
- A native data set was collected to 2.3 Å resolution.
Main Results:
- Crystals belonged to space group P4(1)2(1)2 or P4(3)2(1)2.
- Unit-cell parameters were a = b = 51.61 Å and c = 256.16 Å.
- The crystal structure revealed two protein molecules per asymmetric unit.
Conclusions:
- The successful crystallization and data collection of Saccharomyces cerevisiae Atg10 enable further structural determination.
- This work lays the foundation for understanding the molecular mechanisms of Atg10-mediated conjugation.
- Structural insights into Atg10 will advance research in autophagy and related cellular processes.
