1S68

Structure and Mechanism of RNA Ligase

Summary for 1S68

• Entry DOI: 10.2210/pdb1s68/pdb
• Descriptor: RNA Ligase 2, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: ribonucleic acid ligase, rna repair, t4, ligase
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 1
• Total formula weight: 28677.55

Authors

Ho, C.K.,Wang, L.K.,Lima, C.D.,Shuman, S. (deposition date: 2004-01-22, release date: 2004-02-24, Last modification date: 2024-02-14)

Primary citation

Ho, C.K.,Wang, L.K.,Lima, C.D.,Shuman, S.
Structure and mechanism of RNA ligase.
Structure, 12:327-339, 2004

PubMed Abstract: T4 RNA ligase 2 (Rnl2) exemplifies an RNA ligase family that includes the RNA editing ligases (RELs) of Trypanosoma and Leishmania. The Rnl2/REL enzymes are defined by essential signature residues and a unique C-terminal domain, which we show is essential for sealing of 3'-OH and 5'-PO4 RNA ends by Rnl2, but not for ligase adenylation or phosphodiester bond formation at a preadenylated AppRNA end. The N-terminal segment Rnl2(1-249) of the 334 aa Rnl2 protein comprises an autonomous adenylyltransferase/AppRNA ligase domain. We report the 1.9 A crystal structure of the ligase domain with AMP bound at the active site, which reveals a shared fold, catalytic mechanism, and evolutionary history for RNA ligases, DNA ligases, and mRNA capping enzymes.

PubMed: 14962393
DOI: 10.1016/S0969-2126(04)00023-1

Experimental method

X-RAY DIFFRACTION (1.9 Å)