抄録
Recent exponential increase of three-dimensional structural information by structural genomics revealed that a lot of proteins from hyper-thermophilic organisms have oligomeric structures. Based on these findings, it has been proposed that oligomerization is one of the strategies for enhancing thermostability of proteins in thermophilic organism. Here I describe how oligomerization contributes to the thermostability in protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii from its crystal structural and mutational analyses.
