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Prr1 Coat Protein Binding to its Translational Operator
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
(Latvian Biomedical Research and Study Center)
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
2013 (English)In: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 69, 367-372 p.Article in journal (Refereed) Published
Abstract [en]

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 RNAsegment 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.

Place, publisher, year, edition, pages
2013. Vol. 69, 367-372 p.
Keyword [en]
PRR1, virus, coat protein, RNA
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-135156DOI: 10.1107/S0907444912047464ISI: 000316742700006OAI: oai:DiVA.org:uu-135156DiVA: diva2:374546
Funder
Swedish Research Council
Available from: 2010-12-06 Created: 2010-12-06 Last updated: 2017-12-12Bibliographically approved
In thesis
1. Structural Studies of Bacteriophage PRR1 and HIV-1 protease
Open this publication in new window or tab >>Structural Studies of Bacteriophage PRR1 and HIV-1 protease
2010 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Viruses are a diverse genera of organisms adapted to thrive in many different hosts from prokaryotic to eukaryotic.

We present here the structure of bacteriophage PRR1 virus-like particle (VLP), belonging to Leviviridae family. Our structure reveals calcium ions in the VLP. Metal ions are rare in the VLP among the Leviviridae and the calcium ions were found to affect VLP stability. Gene expression in Leviviridae is controlled by a specific interaction between the viral coat protein that assembles to create the VLP, and the genomic RNA. This interaction has been thoroughly studied for the levivirus MS2 but other structural data are scarce. We have solved the structure of PRR1 VLP in complex with its RNA operator stem-loop. Binding of the stem-loop in PRR1 shows similarities to MS2 but also a different arrangement of the nucleotides, in the area of the loop that we could interpret, compared to MS2. The structures of PRR1 increase our knowledge about translational control in Leviviridae and add new information about particle stability within this family.

The other virus we investigated is the more infamous human pathogen, the HIV. Because of the high mutation rate of HIV new drugs are needed on a continuous basis. We describe here the structure of two new protease inhibitors bound to the HIV-1 protease and compare them with two previously published inhibitors. Due to an extended P1´site the new compounds are able to exploit a new interaction to Phe53 in the protease structure.

Place, publisher, year, edition, pages
Uppsala: Uppsala Universitatis Upsaliensis, 2010. 56 p.
Series
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1651-6214 ; 794
Keyword
PRR1, HIV, Structural Biology, X-ray crystallography, PRR1, HIV-1 protease, NCS, crystallography, inhibitor, virus, bacteriophage, X-ray crystallography
National Category
Microbiology in the medical area Cell and Molecular Biology
Identifiers
urn:nbn:se:uu:diva-135159 (URN)978-91-554-7975-6 (ISBN)
Public defence
2011-01-26, B41, BMC, Husargatan 3, Uppsala, 13:00 (English)
Opponent
Supervisors
Note

Felaktigt tryckt som Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology 724

Available from: 2011-01-05 Created: 2010-12-06 Last updated: 2012-09-18Bibliographically approved

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Liljas, Lars

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