The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family

Proc Natl Acad Sci U S A. 2012 Feb 14;109(7):2296-301. doi: 10.1073/pnas.1116827109. Epub 2012 Jan 27.

Abstract

Pnkp is the end-healing and end-sealing component of an RNA repair system present in diverse bacteria from ten different phyla. To gain insight to the mechanism and evolution of this repair system, we determined the crystal structures of the ligase domain of Clostridium thermocellum Pnkp in three functional states along the reaction pathway: apoenzyme, ligase • ATP substrate complex, and covalent ligase-AMP intermediate. The tertiary structure is composed of a classical ligase nucleotidyltransferase module that is embellished by a unique α-helical insert module and a unique C-terminal α-helical module. Structure-guided mutational analysis identified active site residues essential for ligase adenylylation. Pnkp defines a new RNA ligase family with signature structural and functional properties.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Clostridium thermocellum / enzymology*
  • Crystallization
  • Models, Molecular
  • RNA Ligase (ATP) / chemistry
  • RNA Ligase (ATP) / metabolism*

Substances

  • RNA Ligase (ATP)

Associated data

  • PDB/3TY5
  • PDB/3TY8
  • PDB/3TY9