Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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
