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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
来源:
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.
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页码:616 / 627
页数:12
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