6.5.1.4: RNA 3'-terminal-phosphate cyclase (ATP)
This is an abbreviated version!
For detailed information about RNA 3'-terminal-phosphate cyclase (ATP), go to the full flat file.
Word Map on EC 6.5.1.4
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6.5.1.4
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phosphodiester
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cyclization
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ligases
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nucleotidylation
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adenylylation
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cyclases
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polynucleotide
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eucarya
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pre-rrna
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oligoribonucleotides
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ribozyme
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3',5'-phosphodiester
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alpha-32patp
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cyclase-like
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2'-phosphate
- 6.5.1.4
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phosphodiester
-
cyclization
- ligases
-
nucleotidylation
-
adenylylation
- cyclases
- polynucleotide
- eucarya
- pre-rrna
- oligoribonucleotides
-
ribozyme
-
3',5'-phosphodiester
-
alpha-32patp
-
cyclase-like
-
2'-phosphate
Reaction
Synonyms
PH1529, Rcl1p, RNA 3'-phosphate cyclase, RNA 3'-teminal phosphate cyclase, RNA 3'-terminal phosphate cyclase, RNA 3'-terminal phosphate cylase, RNA cyclase, RNA-3'-phosphate cyclase, RNL, Rtc, Rtc1, RtcA, St-Rtc
ECTree
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Crystallization
Crystallization on EC 6.5.1.4 - RNA 3'-terminal-phosphate cyclase (ATP)
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hanging drop vapor diffusion technique, 2 orthorhombic crystal forms, space group P2(1)2(1)2(1), unit-cell dimensions a : 101.8 A, b : 126.6 A and c : 128.8 A, and P2(1)2(1)2 with unit cell dimensions a : 125.8 A, b : 133.5 A, c : 51.0 A
crystal structure of the enzyme in complex with a 3'-phosphate terminated RNA and adenosine in the AMP-binding pocket
crystallized in the states St-Rtc, St-Rtc+Mn, St-Rtc+ATP, St-Rtc+AMP and St-Rtc-AMP
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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
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