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.
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
↑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