4qjt

Crystal structure of Elongation Factor 4 (EF4/LepA) bound to the Thermus thermophilus 70S ribosome, 30S subunit of the 70S ribosome

spinqualitylabelsall models 4qjt, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qjt is a 25 chain structure with sequence from [1] and Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP, MG, SF4, ZN NonStd Res: 4SU, 5MU, 7MG, F3O, MIA, PSU Related: 4qjs, 4w2e Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Elongation factor 4 (EF4/LepA) is a highly conserved guanosine triphosphatase translation factor. It was shown to promote back-translocation of tRNAs on posttranslocational ribosome complexes and to compete with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis. Here, we report a crystal structure of EF4-guanosine diphosphate bound to the Thermus thermophilus ribosome with a P-site tRNA at 2.9 angstroms resolution. The C-terminal domain of EF4 reaches into the peptidyl transferase center and interacts with the acceptor stem of the peptidyl-tRNA in the P site. The ribosome is in an unusual state of ratcheting with the 30S subunit rotated clockwise relative to the 50S subunit, resulting in a remodeled decoding center. The structure is consistent with EF4 functioning either as a back-translocase or a ribosome sequester. Ribosome structure. Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome.,Gagnon MG, Lin J, Bulkley D, Steitz TA Science. 2014 Aug 8;345(6197):684-7. doi: 10.1126/science.1253525. PMID:25104389 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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