1S7N

Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA free sulfhydryl)

Summary for 1S7N

• Entry DOI: 10.2210/pdb1s7n/pdb
• Related: 1S7F 1S7K 1S7L
• Descriptor: acetyl transferase, COENZYME A (3 entities in total)
• Functional Keywords: acetyltransferase, gnat, alpha-n-protein acetyltransferase, coenzyme a, l7/l12, transferase
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 4
• Total formula weight: 86721.22

Authors

Vetting, M.W.,de Carvalho, L.P.,Roderick, S.L.,Blanchard, J.S. (deposition date: 2004-01-29, release date: 2005-03-15, Last modification date: 2023-08-23)

Primary citation

Vetting, M.W.,de Carvalho, L.P.,Roderick, S.L.,Blanchard, J.S.
A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium.
J.Biol.Chem., 280:22108-22114, 2005

PubMed 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.

PubMed: 15817456
DOI: 10.1074/jbc.M502401200

Experimental method

X-RAY DIFFRACTION (2.1 Å)