CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.360 | Dihydrodipicolinate Reductase; domain 2 |
|
3.30.360.20 | RNA 3'-terminal phosphate cyclase, insert domain |
Domain Context
CATH Clusters
| Superfamily | RNA 3'-terminal phosphate cyclase, insert domain |
| Functional Family | RNA 3'-terminal phosphate cyclase |
Enzyme Information
| 6.5.1.4 |
RNA 3'-terminal-phosphate cyclase (ATP).
based on mapping to UniProt P46849
ATP + (RNA)-3'-(3'-phospho-ribonucleoside) = AMP + diphosphate + (RNA)- 3'-(2',3'-cyclophospho)-ribonucleoside.
-!- The enzyme converts the 3'-terminal phosphate of various RNA substrates into the 2',3'-cyclic phosphodiester in an ATP-dependent reaction. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a histidine residue. -!- The adenylate group is then transferred to the 3'-phosphate terminus of the substrate, forming the capped structure (RNA)- 3'-(5'-diphosphoadenosine). -!- Finally, the enzyme catalyzes an attack of the vicinal O-2' on the 3'-phosphorus, which results in formation of cyclic phosphate and release of the adenylate. -!- The enzyme also has a polynucleotide 5' adenylation activity. -!- Cf. EC 6.5.1.5.
|
UniProtKB Entries (1)
| P46849 |
RTCA_ECOLI
Escherichia coli K-12
RNA 3'-terminal phosphate cyclase
|
PDB Structure
| PDB | 3TUT |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structures of RNA 3'-phosphate cyclase bound to ATP reveal the mechanism of nucleotidyl transfer and metal-assisted catalysis.
Proc.Natl.Acad.Sci.USA
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