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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.77 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
2.1.1.77 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

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

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.77 Sulfurisphaera tokodaii
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-
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Subunits

EC Number Subunits Comment Organism
2.1.1.77 hexamer cooperative hexamerization occurs via interactions of „hot spot" residues Sulfurisphaera tokodaii
2.1.1.77 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

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

Temperature Stability [°C]

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