Brownian Dynamics Study of the Association Between the 70S Ribosome and Elongation Factor G

被引:16
|
作者
Dlugosz, Maciej [1 ]
Huber, Gary A. [2 ]
McCammon, J. Andrew [2 ,3 ,4 ,5 ]
Trylska, Joanna [1 ]
机构
[1] Univ Warsaw, Interdisciplinary Ctr Math & Computat Modeling, Warsaw, Poland
[2] Univ Calif San Diego, Howard Hughes Med Inst, La Jolla, CA 92093 USA
[3] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
[4] Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA
[5] Univ Calif San Diego, Ctr Theoret & Biol Phys, La Jolla, CA 92093 USA
关键词
Brownian dynamics; 70S ribosome; translation; PROTEIN-PROTEIN ASSOCIATION; TRANSFER-RNA MOVEMENT; METAL-ION BINDING; EF-G; CRYSTAL-STRUCTURE; STRUCTURAL DYNAMICS; MOLECULAR MIMICRY; DIFFUSIONAL ENCOUNTER; ANGSTROM RESOLUTION; BACTERIAL RIBOSOME;
D O I
10.1002/bip.21619
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein synthesis on the ribosome involves a number of external protein factors that bind at its functional sites. One key factor is the elongation factor G (EF-G) that facilitates the translocation of transfer RNAs between their binding sites, as well as advancement of the messenger RNA by one codon. The details of the EF-G/ribosome diffusional encounter and EF-G association pathway still remain unanswered. Here, we applied Brownian dynamics methodology to study bimolecular association in the bacterial EF-G/70S ribosome system. We estimated the EF-G association rate constants at 150 and 300 mM monovalent ionic strengths and obtained reasonable agreement with kinetic experiments. We have also elucidated the details of EF-G/ribosome association paths and found that positioning of the L11 protein of the large ribosomal subunit is likely crucial for EF-G entry to its binding site. (C) 2011 Wiley Periodicals, Inc. Biopolymers 95: 616-627, 2011.
引用
收藏
页码:616 / 627
页数:12
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