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Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
Published on: June 28, 2013
Preliminary crystallographic analysis of the major capsid protein P2 of the lipid-containing bacteriophage PM2
Nicola G A Abrescia1, Hanna M Kivelä, Jonathan M Grimes
1Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, England.
Abstract:
PM2 (Corticoviridae) is a dsDNA bacteriophage which contains a lipid membrane beneath its icosahedral capsid. In this respect it resembles bacteriophage PRD1 (Tectiviridae), although it is not known whether the similarity extends to the detailed molecular architecture of the virus, for instance the fold of the major coat protein P2. Structural analysis of PM2 has been initiated and virus-derived P2 has been crystallized by sitting-nanodrop vapour diffusion. Crystals of P2 have been obtained in space group P2(1)2(1)2, with two trimers in the asymmetric unit and unit-cell parameters a = 171.1, b = 78.7, c = 130.1 A. The crystals diffract to 4 A resolution at the ESRF BM14 beamline (Grenoble, France) and the orientation of the non-crystallographic threefold axes, the spatial relationship between the two trimers and the packing of the trimers within the unit cell have been determined. The trimers form tightly packed layers consistent with the crystal morphology, possibly recapitulating aspects of the arrangement of subunits in the virus.
Insights
Structural analysis of bacteriophage PM2 (Corticoviridae) reveals insights into its major coat protein P2. Crystallization and diffraction studies determined the arrangement of P2 trimers, offering clues to the virus
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- PM2 (Corticoviridae) is a dsDNA bacteriophage with a unique lipid membrane beneath its icosahedral capsid.
- PM2 shares structural similarities with bacteriophage PRD1 (Tectiviridae), but detailed molecular architecture, including the major coat protein P2 fold, remains uncharacterized.
Purpose of the Study:
- To initiate structural analysis of bacteriophage PM2.
- To determine the structure and arrangement of the major coat protein P2.
Main Methods:
- Purification and crystallization of virus-derived P2 protein using sitting-nanodrop vapour diffusion.
- X-ray diffraction analysis of P2 crystals to 4 A resolution at the ESRF BM14 beamline.
Main Results:
- P2 protein crystallized in space group P2(1)2(1)2 with two trimers in the asymmetric unit.
- Unit-cell parameters: a = 171.1, b = 78.7, c = 130.1 A.
- The orientation of non-crystallographic threefold axes, spatial relationship between trimers, and packing within the unit cell were determined, revealing tightly packed layers.
Conclusions:
- The crystal packing of P2 trimers may reflect the arrangement of subunits within the intact PM2 virion.
- This study provides foundational structural data for bacteriophage PM2, enabling comparisons with related viruses like PRD1.
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