The pleuromutilin drugs tiamulin and valnemulin bind to the RNA at the peptidyl transferase centre on the ribosome

2008 ◽  
Vol 41 (5) ◽  
pp. 1091-1099 ◽  
Author(s):  
Susan M. Poulsen ◽  
Märit Karlsson ◽  
Lena B. Johansson ◽  
Birte Vester
Keyword(s):  
Peptidyl Transferase ◽  
Peptidyl Transferase Centre

Structure of a conserved RNA component of the peptidyl transferase centre

1997 ◽  
Vol 4 (10) ◽  
pp. 775-778 ◽  
Author(s):  
Elisabetta Viani Puglisi ◽  
Rachel Green ◽  
Harry F. Noller ◽  
Joseph D. Puglisi
Keyword(s):  
Peptidyl Transferase ◽  
Peptidyl Transferase Centre

A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome

Nature ◽  
1995 ◽  
Vol 377 (6547) ◽  
pp. 309-314 ◽  
Author(s):  
Raymond R. Samaha ◽  
Rachel Green ◽  
Harry F. Noller
Keyword(s):  
Base Pair ◽  
23S Rrna ◽  
Peptidyl Transferase ◽  
Peptidyl Transferase Centre

Identifying the peptidyl transferase centre

1982 ◽  
Vol 7 (11) ◽  
pp. 385-386 ◽  
Author(s):  
R.A. Garrett ◽  
Paul Wooley
Keyword(s):  
Peptidyl Transferase ◽  
Peptidyl Transferase Centre

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

2005 ◽  
Vol 33 (3) ◽  
pp. 488-492 ◽  
Author(s):  
A. Bashan ◽  
A. Yonath
Keyword(s):  
Bond Formation ◽  
Peptide Bond ◽  
Trigger Factor ◽  
Chain Elongation ◽  
Peptide Bond Formation ◽  
Peptidyl Transferase ◽  
Chemical Catalysis ◽  
Nascent Chain ◽  
Peptidyl Transferase Centre ◽  
Folding Space

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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