A novel dimeric structure of the RimL Nα-acetyltransferase from Salmonella typhimurium

Matthew W. Vetting, Luiz Pedro S. De Carvalho, Steven L. Roderick, John S. Blanchard

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

RimL is responsible for converting the prokaryotic ribosomal protein from L12 to L7 by acetylation of its N-terminal amino group. We demonstrate that purified RimL is capable of posttranslationally acetylating L12, exhibiting a Vmax of 21 min-1. We have also determined the apostructure of RimL from Salmonella typhimurium and its complex with coenzyme A, revealing a homodimeric oligomer with structural similarity to other Gcn5-related N-acetyltransferase super-family members. A large central trough located at the dimer interface provides sufficient room to bind both L12 N-terminal helices. Structural and biochemical analysis indicates that RimL proceeds by single-step transfer rather than a covalent-enzyme intermediate. This is the first structure of a Gcn5-related N-acetyltransferase family member with demonstrated activity toward a protein Nα-amino group and is a first step toward understanding the molecular basis for Nαacetylation and its function in cellular regulation.

Original languageEnglish (US)
Pages (from-to)22108-22114
Number of pages7
JournalJournal of Biological Chemistry
Volume280
Issue number23
DOIs
StatePublished - Jun 10 2005

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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