Motion in Release Factor 2 [rf2]

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Classification Known Domain Motion, Partial Refolding of Structure [D-f-2]

1gqe free RF2
1mi6 trace of docked RF2 (Rawat et al.)
1ml5 trace of 70S+RF2 (Klaholz et al.)

A pair of cryo-EM studies of the ribosome indicated significant remodelling of release factor 2 in binding to the ribosome. C-alpha coordinates for the docked rf2 structures are available from the PDB.

Rawat UB, Zavialov AV, Sengupta J, Valle M, Grassucci RA, Linde J, Vestergaard B, Ehrenberg M, Frank J (2003). A cryo-electron microscopic study of ribosome-bound termination factor RF2. Nature 421:87-90. [Medline info for 12511960]
Klaholz BP, Pape T, Zavialov AV, Myasnikov AG, Orlova EV, Vestergaard B, Ehrenberg M, van Heel M (2003). Nature 421:90-4. [Medline info for 12511961]
Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M (2001). Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1. Mol Cell 8:1375-82. [Medline info for 11779511]

GO terms associated with structures
Molecular functiontranslation release factor activity, translation release factor activity, codon specific
Cellular componentcytoplasm
Biological processtranslational termination


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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Release Factor 2 upload [ A ] upload [ A ] 358

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_