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)

Summary for 3IYY

• Entry DOI: 10.2210/pdb3iyy/pdb
• Related: 2AW7 2AWB 2WRJ
• EMDB information: 1363
• Descriptor: 50S ribosomal protein L31, 50S ribosomal protein L5, 30S ribosomal protein S13 (3 entities in total)
• Functional Keywords: ribosomal intersubunit bridges, b1b bridge, ratchet-like motion, ribosomal protein l31, ribosomal protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 3
• Total formula weight: 41349.20

Authors

Shasmal, M.,Chakraborty, B.,Sengupta, J. (deposition date: 2010-07-23, release date: 2010-09-01, Last modification date: 2024-02-21)

Primary citation

Shasmal, M.,Chakraborty, B.,Sengupta, J.
Intrinsic molecular properties of the protein-protein bridge facilitate ratchet-like motion of the ribosome.
Biochem.Biophys.Res.Commun., 399:192-197, 2010

PubMed Abstract: 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.

PubMed: 20643101
DOI: 10.1016/j.bbrc.2010.07.053

Experimental method

ELECTRON MICROSCOPY (10.9 Å)