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

Lowri S. Williams; Vladimir M. Levdikov; Leonid Minakhin; Konstantin Severinov; Alfred A. Antson

doi:10.1107/S174430911302486X

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

Lowri S. Williams, Vladimir M. Levdikov, Leonid Minakhin, Konstantin Severinov, Alfred A. Antson^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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 2.1Å resolution and belonged to space group P4212, with unit-cell parameters a = b = 155.3, c = 115.4Å. The unit-cell content and self-rotation function calculations indicate that the protein forms a circular 12-subunit assembly.

Original language	English
Pages (from-to)	1239-1241
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	69
Issue number	11
DOIs	https://doi.org/10.1107/S174430911302486X
Publication status	Published - Nov 2013

Keywords

Bacteriophage G20C
Putative portal protein
Thermus thermophilus

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10.1107/S174430911302486X

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

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{\AA} resolution and belonged to space group P4212, with unit-cell parameters a = b = 155.3, c = 115.4{\AA}. The unit-cell content and self-rotation function calculations indicate that the protein forms a circular 12-subunit assembly.",

keywords = "Bacteriophage G20C, Putative portal protein, Thermus thermophilus",

author = "Williams, {Lowri S.} and Levdikov, {Vladimir M.} and Leonid Minakhin and Konstantin Severinov and Antson, {Alfred A.}",

year = "2013",

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doi = "10.1107/S174430911302486X",

language = "English",

volume = "69",

pages = "1239--1241",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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12-Fold symmetry of the putative portal protein from the Thermus thermophilus bacteriophage G20C determined by X-ray analysis. / Williams, Lowri S.; Levdikov, Vladimir M.; Minakhin, Leonid et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 69, No. 11, 11.2013, p. 1239-1241.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - 12-Fold symmetry of the putative portal protein from the Thermus thermophilus bacteriophage G20C determined by X-ray analysis

AU - Williams, Lowri S.

AU - Levdikov, Vladimir M.

AU - Minakhin, Leonid

AU - Severinov, Konstantin

AU - Antson, Alfred A.

PY - 2013/11

Y1 - 2013/11

N2 - 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 2.1Å resolution and belonged to space group P4212, with unit-cell parameters a = b = 155.3, c = 115.4Å. The unit-cell content and self-rotation function calculations indicate that the protein forms a circular 12-subunit assembly.

AB - 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 2.1Å resolution and belonged to space group P4212, with unit-cell parameters a = b = 155.3, c = 115.4Å. The unit-cell content and self-rotation function calculations indicate that the protein forms a circular 12-subunit assembly.

KW - Bacteriophage G20C

KW - Putative portal protein

KW - Thermus thermophilus

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U2 - 10.1107/S174430911302486X

DO - 10.1107/S174430911302486X

M3 - Article

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AN - SCOPUS:84887313550

SN - 1744-3091

VL - 69

SP - 1239

EP - 1241

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 11

ER -

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

Abstract

Keywords

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