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Publication Abstract from PubMed
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.
A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium.,Vetting MW, de Carvalho LP, Roderick SL, Blanchard JS J Biol Chem. 2005 Jun 10;280(23):22108-14. Epub 2005 Apr 6. PMID:15817456[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Vetting MW, de Carvalho LP, Roderick SL, Blanchard JS. A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium. J Biol Chem. 2005 Jun 10;280(23):22108-14. Epub 2005 Apr 6. PMID:15817456 doi:10.1074/jbc.M502401200
