Ribosome crystallography: catalysis and evolution of peptide-bond formation, nascent chain elongation and its co-translational folding | Zendy

Anat Bashan | Zendy; Ada Yonath | Zendy

Open Access

Ribosome crystallography: catalysis and evolution of peptide-bond formation, nascent chain elongation and its co-translational folding

Author(s) -

Anat Bashan,

Ada Yonath

Publication year - 2005

Publication title -

biochemical society transactions

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.562

H-Index - 144

eISSN - 1470-8752

pISSN - 0300-5127

DOI - 10.1042/bst0330488

Subject(s) - ribosome , ribozyme , chemistry , peptidyl transferase , folding (dsp implementation) , biophysics , chaperone (clinical) , peptide bond , hairpin ribozyme , protein folding , translational frameshift , crystallography , biochemistry , microbiology and biotechnology , peptide , biology , rna , gene , medicine , pathology , electrical engineering , engineering

A ribosome is a ribozyme polymerizing amino acids, exploiting positional- and substrate-mediated chemical catalysis. We showed that peptide-bond formation is facilitated by the ribosomal architectural frame, provided by a sizable symmetry-related region in and around the peptidyl transferase centre, suggesting that the ribosomal active site was evolved by gene fusion. Mobility in tunnel components is exploited for elongation arrest as well as for trafficking nascent proteins into the folding space bordered by the bacterial chaperone, namely the trigger factor.

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