1TFE

DIMERIZATION DOMAIN OF EF-TS FROM T. THERMOPHILUS

1TFE の概要

• エントリーDOI: 10.2210/pdb1tfe/pdb
• 分子名称: ELONGATION FACTOR TS (2 entities in total)
• 機能のキーワード: elongation factor
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm: P43895
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16728.45

構造登録者

Jiang, Y.,Nock, S.,Nesper, M.,Sprinzl, M.,Sigler, P.B. (登録日: 1996-04-16, 公開日: 1996-11-08, 最終更新日: 2024-10-23)

主引用文献

Jiang, Y.,Nock, S.,Nesper, M.,Sprinzl, M.,Sigler, P.B.
Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus.
Biochemistry, 35:10269-10278, 1996

PubMed Abstract: Elongation factor Ts (EF-Ts) functions as a nucleotide-exchange factor by binding elongation factor Tu (EF-Tu) and accelerating the GDP dissociation from EF-Tu; thus EF-Ts promotes the transition of EF-Tu from the inactive GDP form to the active GTP form. Thermus thermophilus EF-Ts exists as a stable dimer in solution which binds two molecules of EF-Tu to form a (EF-Tu.EF-Ts)2 heterotetramer. Here we report the crystal structure of the dimerization domain of EF-Ts from T. thermophilus refined to 1.7 A resolution. A three-stranded antiparallel beta-sheet from each subunit interacts to form a beta-sandwich that serves as an extensive dimer interface tethered by a disulfide bond. This interface is distinctly different from the predominantly alpha-helical one that stabilizes the EF-Ts dimer from Escherichia coli [Kawashima, T., et al. (1996) Nature 379, 511-518]. To test whether the homodimeric form of T. thermophilus EF-Ts is necessary for catalyzing nucleotide exchange, the present structure was used to design mutational changes within the dimer interface that disrupt the T. thermophilus EF-Ts dimer but not the tertiary structure of the subunits. Surprisingly, EF-Ts monomers created in this manner failed to catalyze nucleotide exchange in EF-Tu, indicating that, in vitro. T. thermophilus EF-Ts functions only as a homodimer.

PubMed: 8756682
DOI: 10.1021/bi960918w

実験手法

X-RAY DIFFRACTION (1.7 Å)