Crystallization and preliminary x-ray diffraction data of the EF-Tu · EF-Ts (EF-T) complex of escherichia coli
نویسندگان
چکیده
منابع مشابه
Crystallization and preliminary X-ray diffraction studies of intact EF-Tu from Thermus aquaticus YT-1.
Many attempts have been made to elucidate the three-dimensional structure from elongation factor Tu, but so far the only crystals suitable for X-ray crystallography contained a partially degraded protein. Here, we report the crystallization of a fully active, intact EF-Tu from thermus aquaticus. The crystals belong to hexagonal space group P6(3)(22) and diffract up to 2.6 A. The cell dimensions...
متن کاملCloning and Characterization of EF-Tu and EF-Ts from Pseudomonas aeruginosa
We have cloned genes encoding elongation factors EF-Tu and EF-Ts from Pseudomonas aeruginosa and expressed and purified the proteins to greater than 95% homogeneity. Sequence analysis indicated that P. aeruginosa EF-Tu and EF-Ts are 84% and 55% identical to E. coli counterparts, respectively. P. aeruginosa EF-Tu was active when assayed in GDP exchange assays. Kinetic parameters for the interact...
متن کاملBacterial Backstabbing: EF-Tu, Brute?
Bacterial type VI secretion is an offensive and defensive weapon that utilizes a molecular warhead to inject toxins into neighboring cells. In this issue of Cell, Whitney et al. report a new class of toxin that disrupts the core metabolism of recipient cells and uncover a surprising requirement for EF-Tu.
متن کاملMechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base.
Nucleotide exchange in elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). Similarly to other GTP-binding proteins, the structural changes in the P loop and the Mg(2+) binding site are known to be important for nucleotide release from EF-Tu. In the present paper, we determine the contribution of the contacts between helix D of EF-Tu at the base side of the nucleotide and ...
متن کاملCrystallization and preliminary X-ray crystallographic analysis of YfcM: an important factor for EF-P hydroxylation
Elongation factor P (EF-P) plays an essential role in the translation of polyproline-containing proteins in bacteria. It becomes functional by the post-translational modification of its highly conserved lysine residue. It is first β-lysylated by PoxA and then hydroxylated by YfcM. In this work, the YfcM protein from Escherichia coli was overexpressed, purified and crystallized. The crystal of Y...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Letters
سال: 1981
ISSN: 0014-5793
DOI: 10.1016/0014-5793(81)80155-x