Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 280, Issue 23, Pages 22108-22114Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M502401200
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- NIAID NIH HHS [AI 60899, AI 33696] Funding Source: Medline
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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 V-max 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 superfamily 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 Gen5-related N-acetyltransferase family member with demonstrated activity toward a protein N(alpha)amino group and is a first step toward understanding the molecular basis for N(alpha)acetylation and its function in cellular regulation.
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