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Molecular architecture and ligand recognition determinants for T4 RNA ligase

  1. Author:
    El Omari, K.
    Ren, J.
    Bird, L. E.
    Bona, M. K.
    Klarmann, G.
    Legrice, S. F. J.
    Stammers, D. K.

  2. Author Address

    Univ Oxford, Wellcome Trust Ctr Human Genet, Div Struct Biol, Oxford OX3 7BN, England. Sci Appl Int Co, Frederick, MD 21702 USA. NCI, HIV Drug Resistance Program, NIH, Frederick, MD 21702 USA Stammers, DK, Univ Oxford, Wellcome Trust Ctr Human Genet, Div Struct Biol, Roosevelt Dr, Oxford OX3 7BN, England
    1. Year: 2006
    2. Date: JAN 20
  2. Journal: Journal of Biological Chemistry
    1. 281
    2. 3
    3. Pages: 1573-1579
  4. Type of Article: Article
  1. Abstract:

    RNA ligase type 1 from bacteriophage T4 ( Rnl1) is involved in countering a host defense mechanism by repairing 5'-PO4 and 3'-OH groups in tRNALys. Rnl1 is widely used as a reagent in molecular biology. Although many structures for DNA ligases are available, only fragments of RNA ligases such as Rnl2 are known. We report the first crystal structure of a complete RNA ligase, Rnl1, in complex with adenosine 5'-(alpha,beta-methylenetriphosphate) (AMPcPP). The N- terminal domain is related to the equivalent region of DNA ligases and Rnl2 and binds AMPcPP but with further interactions from the additional N- terminal 70 amino acids in Rnl1 (via Tyr37 and Arg54) and the C-terminal domain (Gly269 and Asp272). The active site contains two metal ions, consistent with the two-magnesium ion catalytic mechanism. The C-terminal domain represents a new all alpha-helical fold and has a charge distribution and architecture for helix-nucleic acid groove interaction compatible with tRNA binding

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  2. WOS: 000234652000035

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