1PN6

Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.

Summary for 1PN6

• Entry DOI: 10.2210/pdb1pn6/pdb
• Related: 1FNM 1PN7 1PN8
• EMDB information: 1055 1362 1363 1364 1365 1366
• Descriptor: Elongation factor G (1 entity in total)
• Functional Keywords: elongation factor-g, e.coli 70s ribosome, post-termination complex, fitting of crystal structure, cryo-em, biosynthetic protein
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: P13551
• Total number of polymer chains: 1
• Total formula weight: 76910.03

Authors

Valle, M.,Zavialov, A.,Sengupta, J.,Rawat, U.,Ehrenberg, M.,Frank, J. (deposition date: 2003-06-12, release date: 2003-07-15, Last modification date: 2024-02-14)

Primary citation

Valle, M.,Zavialov, A.,Sengupta, J.,Rawat, U.,Ehrenberg, M.,Frank, J.
Locking and Unlocking of Ribosomal Motions
Cell(Cambridge,Mass.), 114:123-134, 2003

PubMed Abstract: During the ribosomal translocation, the binding of elongation factor G (EF-G) to the pretranslocational ribosome leads to a ratchet-like rotation of the 30S subunit relative to the 50S subunit in the direction of the mRNA movement. By means of cryo-electron microscopy we observe that this rotation is accompanied by a 20 A movement of the L1 stalk of the 50S subunit, implying that this region is involved in the translocation of deacylated tRNAs from the P to the E site. These ribosomal motions can occur only when the P-site tRNA is deacylated. Prior to peptidyl-transfer to the A-site tRNA or peptide removal, the presence of the charged P-site tRNA locks the ribosome and prohibits both of these motions.

PubMed: 12859903
DOI: 10.1016/S0092-8674(03)00476-8

Experimental method

ELECTRON MICROSCOPY (10.8 Å)