2UZ8

The crystal structure of p18, human translation elongation factor 1 epsilon 1

2UZ8 の概要

• エントリーDOI: 10.2210/pdb2uz8/pdb
• 分子名称: EUKARYOTIC TRANSLATION ELONGATION FACTOR 1 EPSILON-1, GLYCEROL (3 entities in total)
• 機能のキーワード: protein biosynthesis, aminoacyl-trna synthetase, p18, gst, nuclear protein, elongation factor, rna-binding protein, rna binding protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm: O43324
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40332.74

構造登録者

Kang, B.S.,Kim, K.J.,Kim, M.H.,Oh, Y.S.,Kim, S. (登録日: 2007-04-26, 公開日: 2008-03-25, 最終更新日: 2024-11-20)

主引用文献

Kim, K.J.,Park, M.C.,Choi, S.J.,Oh, Y.S.,Choi, E.C.,Cho, H.J.,Kim, M.H.,Kim, S.H.,Kim, D.W.,Kim, S.,Kang, B.S.
Determination of Three-Dimensional Structure and Residues of the Novel Tumor Suppressor Aimp3/P18 Required for the Interaction with Atm.
J.Biol.Chem., 283:14032-, 2008

PubMed Abstract: Although AIMP3/p18 is normally associated with the multi-tRNA synthetase complex via its specific interaction with methionyl-tRNA synthetase, it also works as a tumor suppressor by interacting with ATM, the upstream kinase of p53. To understand the molecular interactions of AIMP3 and the mechanisms involved, we determined the crystal structure of AIMP3 at 2.0-angstroms resolution and identified its potential sites of interaction with ATM. AIMP3 contains two distinct domains linked by a 7-amino acid (Lys57-Ser63) peptide, which contains a 3(10) helix. The 56-amino acid N-terminal domain consists of two helices into which three antiparallel beta strands are inserted, and the 111-amino acid C-terminal domain contains a bundle of five helices (Thr64-Tyr152) followed by a coiled region (Pro153-Leu169). Structural analyses revealed homologous proteins such as yeast glutamyl-tRNA synthetase, Arc1p, EF1Bgamma, and glutathione S-transferase and suggested two potential molecular binding sites. Moreover, mutations at the C-terminal putative binding site abolished the interaction between AIMP3 and ATM and the ability of AIMP3 to activate p53. Thus, this work identified the two potential molecular interaction sites of AIMP3 and determined the residues critical for its tumor-suppressive activity through the interaction with ATM.

PubMed: 18343821
DOI: 10.1074/JBC.M800859200

実験手法

X-RAY DIFFRACTION (2 Å)