Motion in Release Factor 2 [rf2]

[ jump to morphs ]

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

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

Description
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.

References
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, codon specific, translation release factor activity
Cellular componentcytoplasm
Biological processtranslational termination

Morphs

[ show all images ]
Best representative
Morph Morph name Structure #1 Structure #2 Residues
[ ] [ ]



[help] [home] [movies]
Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu