期刊
BIOPHYSICAL JOURNAL
卷 98, 期 10, 页码 2374-2382出版社
CELL PRESS
DOI: 10.1016/j.bpj.2010.02.012
关键词
-
类别
资金
- Swedish Research Council
- Goran Gustafsson Foundation for Research in Natural Sciences and Medicine
- Knut and Alice Wallenberg Foundation
- Spanish Ministerio de Educacion y Ciencia [BIO2007-63458]
- Generalitat de Catalunya [SGR2009 1352]
- European Community [RII3/CT/2004/5060008]
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 N-15 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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据