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Literature summary for 3.1.21.4 extracted from
- Structures, activity and mechanism of the type IIS restriction endonuclease PaqCI (2023), Nucleic Acids Res., 51, 4467-4487.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| the DNA-free apo-enzyme forms a compact enzyme tetramer in the crystal. Four target recognition domains and four endonuclease domains form a starburst-like structure. The complex with a 50 bp double-stranded DNA construct shows all four target recognition domains within the tetramer are individually engaged with four corresponding double-stranded DNA duplexes | Kinneretia aquatilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Kinneretia aquatilis | A0A2N8KYF9 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lamda phage DNA + H2O | - |
Kinneretia aquatilis | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PaqCI | - |
Kinneretia aquatilis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | enzyme shows a random, sequential mechanism in which one double-stranded DNA at a time is cleaved within a fully-formed reaction synapse containing multiple bound DNA target sites | Kinneretia aquatilis |
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