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Literature summary extracted from

  • Shimizu, S.; Ohki, M.; Ohkubo, N.; Suzuki, K.; Tsunoda, M.; Sekiguchi, T.; Takenaka, A.
    Crystal structures of RNA 3-terminal phosphate cyclase and its complexes with Mg2+ +ATP, ATP or Mn2+ (2008), Nucleic Acids Symp. Ser., 52, 221-222.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.5.1.4 native enzyme, with AMP covalently bound, in complex with AMP, with ATP, or Mn2+, at 2.25 A, 2.25A, 2.9 A, 2.4 A and 3.2 A resolutions, respectively. Upon binding of Mg2+ to residue E10, the triphosphate group of the trapped ATP changes its conformation, with help of ligands R17 and R39. The Nepsilon atom of H307 attacks the alpha-phosphate group to form a new P-N bond. When a truncated RNA is bound, its 3'-phosphate group may be forced to react with the phosphate group of AMP, and the activiated 3'-phosphate group may be attacked by the 2'-hydroxyl group to generate the 2',3'-cyclic phosphodiester Sulfurisphaera tokodaii

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.4 Sulfurisphaera tokodaii
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.5.1.4 ATP + [RNA]-3'-(3'-phospho-ribonucleoside) = AMP + diphosphate + [RNA]-3'-(2',3'-cyclophospho)-ribonucleoside upon binding of Mg2+ to residue E10, the triphosphate group of the trapped ATP changes its conformation, with help of ligands R17 and R39. The Nepsilon atom of H307 attacks the alpha-phosphate group to form a new P-N bond. When a truncated RNA is bound, its 3'-phosphate group may be forced to react with the phosphate group of AMP, and the activated 3'-phosphate group may be attacked by the 2'-hydroxyl group to generate the 2',3'-cyclic phosphodiester Sulfurisphaera tokodaii
a