A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel
نویسندگان
چکیده
منابع مشابه
Statics of the ribosomal exit tunnel: implications for cotranslational peptide folding, elongation regulation, and antibiotics binding.
A sophisticated interplay between the static properties of the ribosomal exit tunnel and its functional role in cotranslational processes is revealed by constraint counting on topological network representations of large ribosomal subunits from four different organisms. As for the global flexibility characteristics of the subunit, the results demonstrate a conserved stable structural environmen...
متن کاملAntibiotics at the Ribosomal Exit Tunnel – Selected Structural Aspects
Ribosomes, which are the target of many antibiotics [1, 2] possess spectacular architecture and inherentmobility, allowing their smooth performance in decoding the genetic information as well as in the formation of the peptide bond and the elongation of the newly synthesized proteins. The site for peptide bond formation (peptidyl transferase center, PTC, is located within a highly conserved pse...
متن کاملA Multiscale Approach to Sampling Nascent Peptide Chains in the Ribosomal Exit Tunnel
We present a new multiscale method that combines all-atom molecular dynamics with coarse-grained sampling, towards the aim of bridging two levels of physiology: the atomic scale of protein side chains and small molecules, and the huge scale of macromolecular complexes like the ribosome. Our approach uses all-atom simulations of peptide (or other ligand) fragments to calculate local 3D spatial p...
متن کاملFolding and escape of nascent proteins at ribosomal exit tunnel.
We investigate the interplay between post-translational folding and escape of two small single-domain proteins at the ribosomal exit tunnel by using Langevin dynamics with coarse-grained models. It is shown that at temperatures lower or near the temperature of the fastest folding, folding proceeds concomitantly with the escape process, resulting in vectorial folding and enhancement of foldabili...
متن کاملThe Ribosomal Exit Tunnel Functions as a Discriminating Gate
Translation of SecM stalls unless its N-terminal part is "pulled" by the protein export machinery. Here we show that the sequence motif FXXXXWIXXXXGIRAGP that includes a specific arrest point (Pro) causes elongation arrest within the ribosome. Mutations that bypass the elongation arrest were isolated in 23S rRNA and L22 r protein. Such suppressor mutations occurred at a few specific residues of...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2003
ISSN: 1362-4962
DOI: 10.1093/nar/gkg945