6eze | pdb_00006eze

The open conformation of E.coli Elongation Factor Tu in complex with GDPNP.

spinqualitylabelsall models 6eze, resolution 2.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6eze is a 2 chain structure with sequence from Escherichia coli (strain k12). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GNP, GOL, MG, PEG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [EFTU2_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118] Publication Abstract from PubMed According to the traditional view, GTPases act as molecular switches, which cycle between distinct 'on' and 'off' conformations bound to GTP and GDP, respectively. Translation elongation factor EF-Tu is a GTPase essential for prokaryotic protein synthesis. In its GTP-bound form, EF-Tu delivers aminoacylated tRNAs to the ribosome as a ternary complex. GTP hydrolysis is thought to cause the release of EF-Tu from aminoacyl-tRNA and the ribosome due to a dramatic conformational change following Pi release. Here, the crystal structure of Escherichia coli EF-Tu in complex with a non-hydrolysable GTP analogue (GDPNP) has been determined. Remarkably, the overall conformation of EF-Tu.GDPNP displays the classical, open GDP-bound conformation. This is in accordance with an emerging view that the identity of the bound guanine nucleotide is not 'locking' the GTPase in a fixed conformation. Using a single-molecule approach, the conformational dynamics of various ligand-bound forms of EF-Tu were probed in solution by fluorescence resonance energy transfer. The results suggest that EF-Tu, free in solution, may sample a wider set of conformations than the structurally well-defined GTP- and GDP-forms known from previous X-ray crystallographic studies. Only upon binding, as a ternary complex, to the mRNA-programmed ribosome, is the well-known, closed GTP-bound conformation, observed. E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form.,Johansen JS, Kavaliauskas D, Pfeil SH, Blaise M, Cooperman BS, Goldman YE, Thirup SS, Knudsen CR Nucleic Acids Res. 2018 Aug 11. pii: 5070485. doi: 10.1093/nar/gky697. PMID:30107565 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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