Literature summary for 2.1.1.77 extracted from

Tanaka, Y.; Tsumoto, K.; Yasutake, Y.; Umetsu, M.; Yao, M.; Fukada, H.; Tanaka, I.; Kumagai, I.
How oligomerization contributes to the thermostability of an archaeon protein: protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii (2004), J. Biol. Chem., 279, 32957-32967.

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, crystal structure at 2.8 A resolution. The monomeric structure of StoPIMT consists of two domains, an AdoMet-dependent methyltransferase fold domain and a distinctive C-terminal alpha-helical domain. Six monomers associate into a hexamer, in which there are three contact regions per monomer, referred to as the major, minor, and C-terminal alpha-helical contact regions	Sulfurisphaera tokodaii
hanging-drop vapour diffusion. Crystal structure shows that the enzyme has a distinctive hexameric structure composed of monomers consisting of two domains and a C-terminal alpha-helical domain	Sulfurisphaera tokodaii

Crystallization (Comment)

Organism

hanging drop vapor diffusion method, crystal structure at 2.8 A resolution. The monomeric structure of StoPIMT consists of two domains, an AdoMet-dependent methyltransferase fold domain and a distinctive C-terminal alpha-helical domain. Six monomers associate into a hexamer, in which there are three contact regions per monomer, referred to as the major, minor, and C-terminal alpha-helical contact regions

Sulfurisphaera tokodaii

hanging-drop vapour diffusion. Crystal structure shows that the enzyme has a distinctive hexameric structure composed of monomers consisting of two domains and a C-terminal alpha-helical domain

Sulfurisphaera tokodaii

Protein Variants

Protein Variants	Comment	Organism
DELTA206-231	hexameric structure and thermostability retained	Sulfurisphaera tokodaii

Organism

Organism	UniProt	Comment	Textmining
Sulfurisphaera tokodaii	-	-	-

Subunits

Subunits	Comment	Organism
hexamer	cooperative hexamerization occurs via interactions of hot spot" residues	Sulfurisphaera tokodaii
hexamer	cooperative hexamerization occurs via interactions of hot spot residues. A couple of interfacial hot spot residues are responsible for enhancing thermostability via oligomerization	Sulfurisphaera tokodaii

Synonyms

Synonyms	Comment	Organism
L-isoaspartyl-O-methyltransferase	-	Sulfurisphaera tokodaii
protein L-isoaspartyl-O-methyltransferase	-	Sulfurisphaera tokodaii
StoPIMT	-	Sulfurisphaera tokodaii

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	a couple of interfacial hot spot residues are responsible for enhancing thermostability via oligomerization	Sulfurisphaera tokodaii