PRR1 coat protein binding to its RNA translational operator

被引:10
|
作者
Persson, Magnus [1 ]
Tars, Kaspars [2 ]
Liljas, Lars [1 ]
机构
[1] Uppsala Univ, Dept Cell & Mol Biol, BMC, S-75124 Uppsala, Sweden
[2] Latvian Biomed Res & Study Ctr, LV-1067 Riga, Latvia
基金
瑞典研究理事会;
关键词
PRR1; calcium ions; molecular replacement; bacteriophages; coat proteins; RNA; RECOMBINANT MS2 CAPSIDS; BACTERIOPHAGE-Q-BETA; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; 3-DIMENSIONAL STRUCTURE; METAL-IONS; COMPLEX; RESOLUTION; SPECIFICITY; GA;
D O I
10.1107/S0907444912047464
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
In small RNA bacteriophages, the genomic RNA binds to the coat proteins when the viral capsid assembles. This is achieved through sequence-specific interactions between a coat-protein dimer and an RNA stem-loop that includes the start codon for the replicase gene. The structure of virus-like particles of the small RNA phage PRR1 bound to an RNA segment corresponding to this stem-loop has been solved and the binding was compared with the related, and better investigated, phage MS2. The overall conformation of the RNA is found to be similar and the residues that are involved in RNA binding in PRR1 are the same as in MS2. The arrangement of the nucleotide bases in the loop of the stem-loop is different, leading to a difference in the stacking at the conserved Tyr86, which is equivalent to Tyr85 in MS2.
引用
收藏
页码:367 / 372
页数:6
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