Article
How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii.
The Journal of biological chemistry - 30 Jul 2004
Tanaka Yoshikazu, Tsumoto Kouhei, Yasutake Yoshiaki, Umetsu Mitsuo, Yao Min, Fukada Harumi, Tanaka Isao, Kumagai Izumi
Abstract excerpt
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...
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