Structure (London), 2004-02, Vol.12 (2), p.327-339
2004
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- Autor(en) / Beteiligte
- Titel
- Structure and Mechanism of RNA Ligase
- Ist Teil von
- Structure (London), 2004-02, Vol.12 (2), p.327-339
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 2004
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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′-PO 4 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 Å 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0969-2126eISSN: 1878-4186DOI: 10.1016/j.str.2004.01.011Titel-ID: cdi_proquest_miscellaneous_80155342
- Format
- –
- Schlagworte
- Adenosine Monophosphate - chemistry, Amino Acid Sequence, Animals, Bacteriophage T4 - enzymology, Crystallography, X-Ray, Leishmania, Leishmania - chemistry, Models, Molecular, Molecular Sequence Data, Mutation, phosphodiester bond, Protein Binding, Protein Structure, Tertiary, RNA Ligase (ATP) - chemistry, Sequence Homology, Amino Acid, Trypanosoma, Trypanosoma - chemistry, Viral Proteins - chemistry