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Literature summary extracted from

  • Shimada, A.; Ishikawa, H.; Nakagawa, N.; Kuramitsu, S.; Masui, R.
     The first crystal structure of an archaeal metallo-beta-lactamase superfamily protein; ST1585 from Sulfolobus tokodaii (2010), Proteins Struct. Funct. Bioinform., 78, 2399-2402.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.2.6 expression in Escherichia coli Sulfurisphaera tokodaii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.2.6 to 1.8 A resolution. The overall structure of ST1585 contains thirteen beta-strands and nine alpha-helices. The asymmetric unit of the crystal contains two monomers, and one cis peptide bond is observed between Pro181 and Val182. The overall structure is made up of an alpha-beta-beta-alpha structure. The two-metal ion-binding center is located at the external edge of the beta-beta sandwich, and two zinc ions are coordinated with conserved amino acid residues located in segments 2 to 5 Sulfurisphaera tokodaii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.6 Zn2+ two zinc ions are coordinated with conserved amino acid residues located in segments 2 to 5 Sulfurisphaera tokodaii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.2.6 34000
-
 x * 34000, calculated Sulfurisphaera tokodaii

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.6 Sulfurisphaera tokodaii Q970L2
-
-

Subunits

EC Number Subunits Comment Organism
3.5.2.6 ? x * 34000, calculated Sulfurisphaera tokodaii

Synonyms

EC Number Synonyms Comment Organism
3.5.2.6 ST1585
-
 Sulfurisphaera tokodaii