2CNM

RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with a bisubstrate inhibitor (Cterm-Arg-Arg-Phe-Tyr-Arg-Ala-N-alpha- acetyl-S-CoA).

2CNM の概要

• エントリーDOI: 10.2210/pdb2cnm/pdb
• 関連するPDBエントリー: 2CNS 2CNT
• 分子名称: MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18, 30S RIBOSOMAL PROTEIN S18, COENZYME A, ... (4 entities in total)
• 機能のキーワード: n-alpha acetylation, gcn5-n-acetyltransferase, ribosomal protein, acetyltransferase, gnat, transferase, acyltransferase
• 由来する生物種: SALMONELLA TYPHIMURIUM LT2; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 59971.07

構造登録者

Vetting, M.W.,Yu, M.,Bareich, D.C.,Blanchard, J.S. (登録日: 2006-05-22, 公開日: 2007-05-22, 最終更新日: 2025-10-01)

主引用文献

Vetting, M.W.,Bareich, D.C.,Yu, M.,Blanchard, J.S.
Crystal Structure of Rimi from Salmonella Typhimurium Lt2, the Gnat Responsible for N{Alpha}- Acetylation of Ribosomal Protein S18.
Protein Sci., 17:1781-1790, 2008

PubMed Abstract: The three ribosomal proteins L7, S5, and S18 are included in the rare subset of prokaryotic proteins that are known to be N(alpha)-acetylated. The GCN5-related N-acetyltransferase (GNAT) protein RimI, responsible for the N(alpha)-acetylation of the ribosomal protein S18, was cloned from Salmonella typhimurium LT2 (RimI(ST)), overexpressed, and purified to homogeneity. Steady-state kinetic parameters for RimI(ST) were determined for AcCoA and a peptide substrate consisting of the first six amino acids of the target protein S18. The crystal structure of RimI(ST) was determined in complex with CoA, AcCoA, and a CoA-S-acetyl-ARYFRR bisubstrate inhibitor. The structures are consistent with a direct nucleophilic addition-elimination mechanism with Glu103 and Tyr115 acting as the catalytic base and acid, respectively. The RimI(ST)-bisubstrate complex suggests that several residues change conformation upon interacting with the N terminus of S18, including Glu103, the proposed active site base, facilitating proton exchange and catalysis.

PubMed: 18596200
DOI: 10.1110/PS.035899.108

実験手法

X-RAY DIFFRACTION (2.6 Å)