Literature summary for 6.5.1.8 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)

Cloned (Comment)	Organism
expression in Escherichia coli	Pyrococcus furiosus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Metals/Ions	Comment	Organism	Structure
Mn2+	prior to binding GTP, a single manganese ion is bound to RtcB	Pyrococcus furiosus

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	Q8U0H4	-	-

Synonyms

Synonyms	Comment	Organism
rtcB	-	Pyrococcus furiosus
tRNA-splicing ligase	-	Pyrococcus furiosus

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Release 2023.1 (January 2023)