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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.
    View publication on PubMedView publication on EuropePMC

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
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-

Synonyms

EC Number Synonyms Comment Organism
6.5.1.8 rtcB
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Pyrococcus furiosus
6.5.1.8 tRNA-splicing ligase
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Pyrococcus furiosus