1S7K

RimL- Ribosomal L7/L12 alpha-N-protein acetyltransferase crystal form 2 (apo)

1S7K の概要

• エントリーDOI: 10.2210/pdb1s7k/pdb
• 関連するPDBエントリー: 1S7F 1S7L 1S7N
• 分子名称: acetyl transferase (2 entities in total)
• 機能のキーワード: acetyltransferase, gnat, alpha-n-protein acetyltransferase, coenzyme a, l7/l12, transferase
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20912.77

構造登録者

Vetting, M.W.,de Carvalho, L.P.,Roderick, S.L.,Blanchard, J.S. (登録日: 2004-01-29, 公開日: 2005-03-15, 最終更新日: 2023-08-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)