PMID:15817456
| Citation |
Vetting, MW, de Carvalho, LP, Roderick, SL and Blanchard, JS (2005) A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium. J. Biol. Chem. 280:22108-14 |
|---|---|
| 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 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 Gcn5-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. |
| Links |
PubMed Online version:10.1074/jbc.M502401200 |
| Keywords |
Acetyltransferases/chemistry; Acetyltransferases/metabolism; Acetyltransferases/physiology; Animals; Bacterial Proteins; Binding Sites; Cattle; Cloning, Molecular; Coenzyme A/chemistry; Crystallography, X-Ray; Dimerization; Escherichia coli/metabolism; Kinetics; Models, Chemical; Models, Molecular; Protein Binding; Protein Conformation; Protein Folding; Protein Isoforms; Protein Processing, Post-Translational; Protein Structure, Tertiary; Salmonella typhimurium/enzymology; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
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