Solution structure of the 2'-5' RNA ligase-like protein from Pyrococcus furiosusSolution structure of the 2'-5' RNA ligase-like protein from Pyrococcus furiosus

Structural highlights

2fyh is a 1 chain structure with sequence from Pyrococcus furiosus DSM 3638. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

THPR_PYRFU Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester. In vitro, ligates 5' and 3' half-tRNA molecules with 2',3'-cyclic phosphate and 5'-hydroxyl termini, respectively, to the product containing the 2'-5' phosphodiester linkage. Ligase activity requires GTP, but GTP hydrolysis is not required for the reaction, which is reversible. Ligase activity is weak compared to the phosphodiesterase activity.[1]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Kanai A, Sato A, Fukuda Y, Okada K, Matsuda T, Sakamoto T, Muto Y, Yokoyama S, Kawai G, Tomita M. Characterization of a heat-stable enzyme possessing GTP-dependent RNA ligase activity from a hyperthermophilic archaeon, Pyrococcus furiosus. RNA. 2009 Mar;15(3):420-31. Epub 2009 Jan 20. PMID:19155324 doi:10.1261/rna.1122109
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