» Articles » PMID: 19004020

Collective Dynamics of the Ribosomal Tunnel Revealed by Elastic Network Modeling

Overview
Journal Proteins
Date 2008 Nov 13
PMID 19004020
Citations 21
Authors
Affiliations
Soon will be listed here.
Abstract

The collective dynamics of the nascent polypeptide exit tunnel are investigated with the computationally efficient elastic network model using normal mode analysis. The calculated normal modes are considered individually and in linear combinations with different coefficients mimicking the phase angles between modes, in order to follow the mechanistic motions of tunnel wall residues. The low frequency fluctuations indicate three distinct regions along the tunnel-the entrance, the neck, and the exit-each having distinctly different domain motions. Generally, the lining of the entrance region moves in the exit direction, with the exit region having significantly larger motions, but in a perpendicular direction, whereas the confined neck region has rotational motions. Especially the universally conserved extensions of ribosomal proteins L4 and L22 located at the narrowest and mechanistically strategic region of tunnel undergo generally anti- or non-correlated motions, which may have an important role in nascent polypeptide gating mechanism. These motions appear to be sufficiently robust so as to be unaffected by the presence of a peptide chain in the tunnel.

Citing Articles

The role of ribosomal protein networks in ribosome dynamics.

Timsit Y, Sergeant-Perthuis G, Bennequin D Nucleic Acids Res. 2025; 53(1.

PMID: 39788545 PMC: 11711686. DOI: 10.1093/nar/gkae1308.


Ratchet, swivel, tilt and roll: a complete description of subunit rotation in the ribosome.

Hassan A, Byju S, Freitas F, Roc C, Pender N, Nguyen K Nucleic Acids Res. 2022; 51(2):919-934.

PMID: 36583339 PMC: 9881166. DOI: 10.1093/nar/gkac1211.


Exploring Allosteric Signaling in the Exit Tunnel of the Bacterial Ribosome by Molecular Dynamics Simulations and Residue Network Model.

Guzel P, Yildirim H, Yuce M, Kurkcuoglu O Front Mol Biosci. 2020; 7:586075.

PMID: 33102529 PMC: 7545307. DOI: 10.3389/fmolb.2020.586075.


Normal Mode Analysis as a Routine Part of a Structural Investigation.

Bauer J, Pavlovic J, Bauerova-Hlinkova V Molecules. 2019; 24(18).

PMID: 31510014 PMC: 6767145. DOI: 10.3390/molecules24183293.


Modeling of Protein Structural Flexibility and Large-Scale Dynamics: Coarse-Grained Simulations and Elastic Network Models.

Kmiecik S, Kouza M, Badaczewska-Dawid A, Kloczkowski A, Kolinski A Int J Mol Sci. 2018; 19(11).

PMID: 30404229 PMC: 6274762. DOI: 10.3390/ijms19113496.


References
1.
Milligan R, Unwin P . Location of exit channel for nascent protein in 80S ribosome. Nature. 1986; 319(6055):693-5. DOI: 10.1038/319693a0. View

2.
Beckmann R, Spahn C, Eswar N, Helmers J, Penczek P, Sali A . Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell. 2001; 107(3):361-72. DOI: 10.1016/s0092-8674(01)00541-4. View

3.
Atilgan A, Durell S, Jernigan R, Demirel M, Keskin O, Bahar I . Anisotropy of fluctuation dynamics of proteins with an elastic network model. Biophys J. 2001; 80(1):505-15. PMC: 1301252. DOI: 10.1016/S0006-3495(01)76033-X. View

4.
Berman H, Westbrook J, Feng Z, Gilliland G, Bhat T, Weissig H . The Protein Data Bank. Nucleic Acids Res. 1999; 28(1):235-42. PMC: 102472. DOI: 10.1093/nar/28.1.235. View

5.
Chennubhotla C, Bahar I . Markov propagation of allosteric effects in biomolecular systems: application to GroEL-GroES. Mol Syst Biol. 2006; 2:36. PMC: 1681507. DOI: 10.1038/msb4100075. View