4v4i | pdb_00004v4i
From Proteopedia
Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements.
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Structural highlights
FunctionRL1_THET2 Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity). Publication Abstract from PubMedOur understanding of the mechanism of protein synthesis has undergone rapid progress in recent years as a result of low-resolution X-ray and cryo-EM structures of ribosome functional complexes and high-resolution structures of ribosomal subunits and vacant ribosomes. Here, we present the crystal structure of the Thermus thermophilus 70S ribosome containing a model mRNA and two tRNAs at 3.7 A resolution. Many structural details of the interactions between the ribosome, tRNA, and mRNA in the P and E sites and the ways in which tRNA structure is distorted by its interactions with the ribosome are seen. Differences between the conformations of vacant and tRNA-bound 70S ribosomes suggest an induced fit of the ribosome structure in response to tRNA binding, including significant changes in the peptidyl-transferase catalytic site. Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements.,Korostelev A, Trakhanov S, Laurberg M, Noller HF Cell. 2006 Sep 22;126(6):1065-77. Epub 2006 Sep 7. PMID:16962654[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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