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Literature summary for 6.5.1.8 extracted from

  • Englert, M.; Xia, S.; Okada, C.; Nakamura, A.; Tanavde, V.; Yao, M.; Eom, S.H.; Konigsberg, W.H.; Soell, D.; Wang, J.
    Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3-terminal phosphate and 5-OH (2012), Proc. Natl. Acad. Sci. USA, 109, 15235-15240.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of RtcB in complex with Mn2+ alone and together with a covalently bound GMP, to 1.6 A and 2.3 A resolution, respectively. The RtcB/Mn2+ structure shows two Mn2+ ions at the active site, and an array of sulfate ions nearby that indicate the binding sites of the RNA phosphate backbone. The structure of the RtcB-GMP/Mn2+ complex reveals the detailed geometry of guanylylation of histidine 404. The enzyme's substrate-induced GTP binding site and the putative reactive RNA ends are in the vicinity of the binuclear Mn2+ active center Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ the RtcB/Mn2+ structure shows two Mn2+ ions at the active site. The enzyme's substrate-induced GTP binding site and the putative reactive RNA ends are in the vicinity of the binuclear Mn2+ active center Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O59245
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Pyrococcus horikoshii DSM 12428 O59245
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Synonyms

Synonyms Comment Organism
RNA-splicing ligase
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Pyrococcus horikoshii