1AIP

EF-TU EF-TS COMPLEX FROM THERMUS THERMOPHILUS

1AIP の概要

• エントリーDOI: 10.2210/pdb1aip/pdb
• 分子名称: ELONGATION FACTOR TU, ELONGATION FACTOR TS (3 entities in total)
• 機能のキーワード: elongation factor, nucleotide exchange, gtp-binding, complex of two elongation factors
• 由来する生物種: Thermus thermophilus; 詳細
• 細胞内の位置: Cytoplasm: P60338 P43895
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 268755.76

構造登録者

Wang, Y.,Jiang, Y.,Meyering-Voss, M.,Sprinzl, M.,Sigler, P.B. (登録日: 1997-04-22, 公開日: 1997-10-22, 最終更新日: 2024-11-13)

主引用文献

Wang, Y.,Jiang, Y.,Meyering-Voss, M.,Sprinzl, M.,Sigler, P.B.
Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.
Nat.Struct.Biol., 4:650-656, 1997

PubMed Abstract: In order to study nucleotide exchange mechanisms in GTP-binding proteins, we have determined the crystal structure of the complex formed by the elongation factor Tu (EF-Tu) and its exchange factor Ts (EF-Ts) from Thermus thermophilus. The complex is a dyad symmetrical heterotetramer in which each EF-Tu, through a bipartite interface, interacts with two subunits of EF-Ts, explaining the need for a dimeric exchange factor. The architecture of the assembly is distinctly different from that of the corresponding heterodimeric E. coli complex, in which the monomeric E. coli EF-Ts remarkably forms essentially the same bipartite interface with EF-Tu through a sequence/structural repeat. GDP is released primarily by a Ts-induced peptide flip in the nucleotide binding pocket that disrupts hydrogen bonds to the phosphates and repositions the peptide carbonyl so as to sterically and electrostatically eject the GDP. The exchange mechanism may have useful implications for receptor-induced exchange in heterotrimeric G proteins.

PubMed: 9253415
DOI: 10.1038/nsb0897-650

実験手法

X-RAY DIFFRACTION (3 Å)