How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii.

@article{Tanaka2004HowOC,
  title={How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii.},
  author={Yoshikazu Tanaka and Kouhei Tsumoto and Yoshiaki Yasutake and Mitsuo Umetsu and Min Li Yao and Harumi Fukada and Isao Tanaka and Izumi Kumagai},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 31},
  pages={32957-67}
}
To study how oligomerization may contribute to the thermostability of archaeon proteins, we focused on a hexameric protein, protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii (StoPIMT). The crystal structure shows that StoPIMT has a distinctive hexameric structure composed of monomers consisting of two domains: an S-adenosylmethionine-dependent methyltransferase fold domain and a C-terminal alpha-helical domain. The hexameric structure includes three interfacial contact regions… CONTINUE READING