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12-Fold symmetry of the putative portal protein from the Thermus thermophilus bacteriophage G20C determined by X-ray analysis

DOI: 10.1107/S174430911302486X DOI Help
PMID: 24192358 PMID Help

Authors: Lowri S. Williams (University of York) , Vladimir Levdikov (University of York) , Leonid Minakhin (Rutgers, The State University of New Jersey) , Konstantin Severinov (Rutgers, The State University of New Jersey; St Petersburg State Polytechnical University) , Alfred A. Antson (University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 69

State: Published (Approved)
Published: November 2013

Open Access Open Access

Abstract: In tailed bacteriophages and several animal viruses, the portal protein forms the gateway through which viral DNA is translocated into the head structure during viral particle assembly. In the mature virion the portal protein exists as a dodecamer, while recombinant portal proteins from several phages, including SPP1 and CNPH82, have been shown to form 13-subunit assemblies. A putative portal protein from the thermostable bacteriophage G20C has been cloned, overexpressed and purified. Crystals of the protein diffracted to 2.1 Å resolution and belonged to space group P4212, with unit-cell parameters a = b = 155.3, c = 115.4 Å. The unit-cell content and self-rotation function calculations indicate that the protein forms a circular 12-subunit assembly.

Journal Keywords: putative portal protein; Thermus thermophilus; bacteriophage G20C

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography