Literature summary extracted from
Desai, K.K.; Bingman, C.A.; Phillips, G.N.; Raines, R.T.
Structures of the noncanonical RNA ligase RtcB reveal the mechanism of histidine guanylylation (2013), Biochemistry, 52, 2518-2525.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
6.5.1.8 |
expression in Escherichia coli |
Pyrococcus furiosus |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
6.5.1.8 |
three structures of RtcB complexes that capture snapshots along the entire guanylylation pathway. RtcB in complex with Mn(II) and GTP analogue guanosine 5'-(alpha-thio)-triphosphate shows that Mn1 is poised to stabilize the pentavalent transition state of guanylylation while a second manganese ion (Mn2) is coordinated to a nonbridging oxygen of the gamma-phosphoryl group. The diphosphate leaving group of 5'-(alpha-thio)-triphosphate is oriented apically to His404 with the epsilon nitrogen poised for in-line attack on the alpha phosphorus atom. The structure of RtcB in complex with 5'-(alpha-thio)-triphosphate also reveals the network of hydrogen bonds that recognize GTP and shows significant conformational changes accompanying the binding of the cofactor. A structure of the enzymic histidine-GMP intermediate depicts the end of the guanylylation pathway |
Pyrococcus furiosus |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
6.5.1.8 |
Mn2+ |
prior to binding GTP, a single manganese ion is bound to RtcB |
Pyrococcus furiosus |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
6.5.1.8 |
Pyrococcus furiosus |
Q8U0H4 |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
6.5.1.8 |
rtcB |
- |
Pyrococcus furiosus |
6.5.1.8 |
tRNA-splicing ligase |
- |
Pyrococcus furiosus |