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The capsid of the small RNA phage PRR1 is stabilized by metal ions.
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.
2008 (English)In: Journal of molecular biology, ISSN 1089-8638, Vol. 383, no 4, 914-22 p.Article in journal (Refereed) Published
Abstract [en]

Many nonenveloped virus particles are stabilized by calcium ions bound in the interfaces between the protein subunits. These ions may have a role in the disassembly process. The small RNA phages of the Leviviridae family have T=3 quasi-symmetry and are unique among simple viruses in that they have a coat protein with a translational repressor activity and a fold that has not been observed in other viruses. The crystal structure of phage PRR1 has been determined to 3.5 A resolution. The structure shows a tentative binding site for a calcium ion close to the quasi-3-fold axis. The RNA-binding surface used for repressor activity is mostly conserved. The structure does not show any significant differences between quasi-equivalent subunits, which suggests that the assembly is not controlled by conformational switches as in many other simple viruses.

Place, publisher, year, edition, pages
2008. Vol. 383, no 4, 914-22 p.
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:uu:diva-104176DOI: 10.1016/j.jmb.2008.08.060ISI: 000260533800015PubMedID: 18786545OAI: oai:DiVA.org:uu-104176DiVA: diva2:219445
Available from: 2009-05-27 Created: 2009-05-27 Last updated: 2011-03-11Bibliographically 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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