Protein Variants | Comment | Organism |
---|---|---|
H337A | His337 is the site covalent guanylylation of RtcB, mutant is inactive | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | absolutely required, assay at 2 mM | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P46850 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O | substrate for ligation is a 20mer RNA strand with 5'-OH and 2',3'-cyclic phosphate ends | Escherichia coli | (ribonucleotide)n+m + GMP + diphosphate | overall reaction | ? | |
5'-guanosyl [RNA ligase]-NT-phosphono-L-histidine + (ribonucleotide)n-3'-phosphate | - |
Escherichia coli | (ribonucleotide)n-3'-(5'-diphosphoguanosine) + [RNA ligase]-L-histidine | RtcB transfers GMP to the RNA 3'-phosphate end | ? | |
GTP + [RNA ligase]-L-histidine | - |
Escherichia coli | 5'-guanosyl [RNA ligase]-NT-phosphono-L-histidine + diphosphate | - |
? | |
additional information | sealing of a 2',3'-cyclic phosphate end by RtcB requires GTP, is contingent on formation of the RtcBGMP adduct, and involves a kinetically valid RNA(3')pp(5')G intermediate. RtcB catalyzes the hydrolysis of a 2',3'-cyclic phosphate to a 3'-phosphate at a rate that is at least as fast as the rate of ligation. NTP requirement for ligation is satisfied by GTP and 6-O-methyl guanosine triphosphate and inosine triphosphate. 6-chloropurine ribonucleoside triphosphate, 2-aminopurine ribonucleoside triphosphate and ATP are inactive | Escherichia coli | ? | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | RtcB guanylylation precedes the cyclic phosphodiesterase and 3'-phosphate ligase steps of the RNA splicing pathway | Escherichia coli |