Essential role of an active-site guanine in glmS ribozyme catalysis

J Am Chem Soc. 2007 Dec 5;129(48):14858-9. doi: 10.1021/ja0768441. Epub 2007 Nov 9.

Abstract

The glmS ribozyme is a catalytic riboswitch that is activated for endonucleolytic cleavage by the coenzyme glucosamine-6-phosphate. Using kinetic assays and X-ray crystallography, we identify an active-site mutation of a conserved guanine that abolishes catalysis without perturbing coenzyme binding. Our results provide evidence that coenzyme function requires a specific nucleobase to interact with the nucleophile of the cleavage reaction.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus anthracis / enzymology
  • Bacillus anthracis / genetics
  • Binding Sites
  • Catalysis
  • Crystallography, X-Ray
  • Guanine / chemistry*
  • Guanine / metabolism*
  • Models, Molecular
  • Molecular Structure
  • Mutation / genetics
  • RNA, Catalytic / chemistry*
  • RNA, Catalytic / genetics
  • RNA, Catalytic / metabolism*
  • Thermoanaerobacter / enzymology
  • Thermoanaerobacter / genetics

Substances

  • RNA, Catalytic
  • Guanine

Associated data

  • PDB/3B4A
  • PDB/3B4B
  • PDB/3B4C