de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression

MPS-Authors

Harms,  Joerg
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50097

Berisio,  Rita
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

Bartels,  Heike
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50157

Franceschi,  Francois
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

Yonath,  Ada
Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Bashan, A., Agmon, I., Zarivach, R., Schluenzen, F., Harms, J., Berisio, R., et al. (2003). Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression. Molecular Cell, 11(1), 91-102. doi:10.1016/S1097-2765(03)00009-1.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-8B09-5
Abstract
Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3′ end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this