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TitleIntrinsic molecular properties of the protein-protein bridge facilitate ratchet-like motion of the ribosome.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 399, Issue 2, Page 192-197, Year 2010
Publish dateAug 20, 2010
AuthorsManidip Shasmal / Biprashekhar Chakraborty / Jayati Sengupta /
PubMed AbstractThe ribosomal intersubunit bridges maintain the overall architecture of the ribosome and thereby play a pivotal role in the dynamics of translation. The only protein-protein bridge, b1b, is formed by ...The ribosomal intersubunit bridges maintain the overall architecture of the ribosome and thereby play a pivotal role in the dynamics of translation. The only protein-protein bridge, b1b, is formed by the two proteins, S13 and L5 of the small and large ribosomal subunits, respectively. B1b absorbs the largest movement during ratchet-like motion, and its two proteins reorganize in different constellations during this motion of the ribosome. Our results in this study of b1b in the Escherichia coli 70S ribosome suggest that the intrinsic molecular features of the bridging proteins allow the bridge to modulate the ratchet-like motion in a controlled manner. Additionally, another large subunit protein, L31, seems to participate with S13 and L5 in the formation, dynamics, and stabilization of this bridge.
External linksBiochem Biophys Res Commun / PubMed:20643101
MethodsEM (single particle)
Resolution9 - 10.9 Å
Structure data

PDB-3iyx:
Coordinates of the b1b bridge-forming protein structures fitted into the Cryo-EM map of E.coli 70S ribosome (EMD-1056)
Method: ELECTRON MICROSCOPY / Resolution: 9.0 Å

PDB-3iyy:
Coordinates of the b1b bridge-forming protein structures fitted into the Cryo-EM map of EFG.GDPNP-bound E.coli 70S ribosome(EMD-1363)
Method: ELECTRON MICROSCOPY / Resolution: 10.9 Å

Source
  • escherichia coli (E. coli)
KeywordsRIBOSOMAL PROTEIN / Ribosomal intersubunit bridges / B1b-bridge / Ratchet-like motion / Ribosomal protein L31 / B1b Bridge

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