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Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation.
- Source :
-
Biophysical journal [Biophys J] 2010 May 19; Vol. 98 (10), pp. 2374-82. - Publication Year :
- 2010
-
Abstract
- Ribosomal protein L12 is a two-domain protein that forms dimers mediated by its N-terminal domains. A 20-residue linker separates the N- and C-terminal domains. This linker results in a three-lobe topology with significant flexibility, known to be critical for efficient translation. Here we present an ensemble model of spatial distributions and correlation times for the domain reorientations of L12 that reconciles experimental data from small-angle x-ray scattering and nuclear magnetic resonance. We generated an ensemble of L12 conformations in which the structure of each domain is fixed but the domain orientations are variable. The ensemble reproduces the small-angle x-ray scattering data and the optimized correlation times of its reorientational eigenmodes fit the (15)N relaxation data. The ensemble model reveals intrinsic conformational properties of L12 that help explain its function on the ribosome. The two C-terminal domains sample a large volume and extend further away from the ribosome anchor than expected for a random-chain linker, indicating that the flexible linker has residual order. Furthermore, the distances between each C-terminal domain and the anchor are anticorrelated, indicating that one of them is more retracted on average. We speculate that these properties promote the function of L12 to recruit translation factors and control their activity on the ribosome.<br /> (Copyright 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.)
- Subjects :
- Escherichia coli Proteins chemistry
Nuclear Magnetic Resonance, Biomolecular
Prokaryotic Initiation Factor-2
Protein Conformation radiation effects
Protein Folding radiation effects
Protein Structure, Tertiary
Ribosomal Proteins chemistry
Ribosomal Proteins metabolism
Ribosomes metabolism
Magnetic Resonance Spectroscopy adverse effects
Ribosomal Proteins radiation effects
Ribosomes radiation effects
Scattering, Small Angle
X-Rays
Subjects
Details
- Language :
- English
- ISSN :
- 1542-0086
- Volume :
- 98
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Biophysical journal
- Publication Type :
- Academic Journal
- Accession number :
- 20483347
- Full Text :
- https://doi.org/10.1016/j.bpj.2010.02.012