The putative small terminase from the thermophilic dsDNA bacteriophage G20C is a nine-subunit oligomer

Juan Loredo-Varela; Maria Chechik; Vladimir M. Levdikov; Ahmad Abd-El-Aziz; Leonid Minakhin; Konstantin Severinov; Callum Smits; Alfred A. Antson

doi:10.1107/S1744309113017016

The putative small terminase from the thermophilic dsDNA bacteriophage G20C is a nine-subunit oligomer

Juan Loredo-Varela, Maria Chechik, Vladimir M. Levdikov, Ahmad Abd-El-Aziz, Leonid Minakhin, Konstantin Severinov, Callum Smits, Alfred A. Antson^*

^*Corresponding author for this work

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

Abstract

The assembly of double-stranded DNA bacteriophages is dependent on a small terminase protein that normally plays two important roles. Firstly, the small terminase protein specifically recognizes viral DNA and recruits the large terminase protein, which makes the initial cut in the dsDNA. Secondly, once the complex of the small terminase, the large terminase and the DNA has docked to the portal protein, and DNA translocation into a preformed empty procapsid has begun, the small terminase modulates the ATPase activity of the large terminase. Here, the putative small terminase protein from the thermostable bacteriophage G20C, which infects the Gram-negative eubacterium Thermus thermophilus, has been produced, purified and crystallized. Size-exclusion chromatography-multi-angle laser light scattering data indicate that the protein forms oligomers containing nine subunits. Crystals diffracting to 2.8Å resolution have been obtained. These belonged to space group P212121, with unit-cell parameters a = 94.31, b = 125.6, c = 162.8Å. The self-rotation function and Matthews coefficient calculations are consistent with the presence of a nine-subunit oligomer in the asymmetric unit.

Original language	English
Pages (from-to)	876-879
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	69
Issue number	8
DOIs	https://doi.org/10.1107/S1744309113017016
Publication status	Published - Aug 2013

Keywords

bacteriophage G20C
putative small terminase
Thermus thermophilus

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Loredo-Varela, J., Chechik, M., Levdikov, V. M., Abd-El-Aziz, A., Minakhin, L., Severinov, K., Smits, C., & Antson, A. A. (2013). The putative small terminase from the thermophilic dsDNA bacteriophage G20C is a nine-subunit oligomer. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69(8), 876-879. https://doi.org/10.1107/S1744309113017016

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title = "The putative small terminase from the thermophilic dsDNA bacteriophage G20C is a nine-subunit oligomer",

abstract = "The assembly of double-stranded DNA bacteriophages is dependent on a small terminase protein that normally plays two important roles. Firstly, the small terminase protein specifically recognizes viral DNA and recruits the large terminase protein, which makes the initial cut in the dsDNA. Secondly, once the complex of the small terminase, the large terminase and the DNA has docked to the portal protein, and DNA translocation into a preformed empty procapsid has begun, the small terminase modulates the ATPase activity of the large terminase. Here, the putative small terminase protein from the thermostable bacteriophage G20C, which infects the Gram-negative eubacterium Thermus thermophilus, has been produced, purified and crystallized. Size-exclusion chromatography-multi-angle laser light scattering data indicate that the protein forms oligomers containing nine subunits. Crystals diffracting to 2.8{\AA} resolution have been obtained. These belonged to space group P212121, with unit-cell parameters a = 94.31, b = 125.6, c = 162.8{\AA}. The self-rotation function and Matthews coefficient calculations are consistent with the presence of a nine-subunit oligomer in the asymmetric unit.",

keywords = "bacteriophage G20C, putative small terminase, Thermus thermophilus",

author = "Juan Loredo-Varela and Maria Chechik and Levdikov, {Vladimir M.} and Ahmad Abd-El-Aziz and Leonid Minakhin and Konstantin Severinov and Callum Smits and Antson, {Alfred A.}",

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Loredo-Varela, J, Chechik, M, Levdikov, VM, Abd-El-Aziz, A, Minakhin, L, Severinov, K, Smits, C & Antson, AA 2013, 'The putative small terminase from the thermophilic dsDNA bacteriophage G20C is a nine-subunit oligomer', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 69, no. 8, pp. 876-879. https://doi.org/10.1107/S1744309113017016

TY - JOUR

T1 - The putative small terminase from the thermophilic dsDNA bacteriophage G20C is a nine-subunit oligomer

AU - Loredo-Varela, Juan

AU - Chechik, Maria

AU - Levdikov, Vladimir M.

AU - Abd-El-Aziz, Ahmad

AU - Minakhin, Leonid

AU - Severinov, Konstantin

AU - Smits, Callum

AU - Antson, Alfred A.

PY - 2013/8

Y1 - 2013/8

N2 - The assembly of double-stranded DNA bacteriophages is dependent on a small terminase protein that normally plays two important roles. Firstly, the small terminase protein specifically recognizes viral DNA and recruits the large terminase protein, which makes the initial cut in the dsDNA. Secondly, once the complex of the small terminase, the large terminase and the DNA has docked to the portal protein, and DNA translocation into a preformed empty procapsid has begun, the small terminase modulates the ATPase activity of the large terminase. Here, the putative small terminase protein from the thermostable bacteriophage G20C, which infects the Gram-negative eubacterium Thermus thermophilus, has been produced, purified and crystallized. Size-exclusion chromatography-multi-angle laser light scattering data indicate that the protein forms oligomers containing nine subunits. Crystals diffracting to 2.8Å resolution have been obtained. These belonged to space group P212121, with unit-cell parameters a = 94.31, b = 125.6, c = 162.8Å. The self-rotation function and Matthews coefficient calculations are consistent with the presence of a nine-subunit oligomer in the asymmetric unit.

AB - The assembly of double-stranded DNA bacteriophages is dependent on a small terminase protein that normally plays two important roles. Firstly, the small terminase protein specifically recognizes viral DNA and recruits the large terminase protein, which makes the initial cut in the dsDNA. Secondly, once the complex of the small terminase, the large terminase and the DNA has docked to the portal protein, and DNA translocation into a preformed empty procapsid has begun, the small terminase modulates the ATPase activity of the large terminase. Here, the putative small terminase protein from the thermostable bacteriophage G20C, which infects the Gram-negative eubacterium Thermus thermophilus, has been produced, purified and crystallized. Size-exclusion chromatography-multi-angle laser light scattering data indicate that the protein forms oligomers containing nine subunits. Crystals diffracting to 2.8Å resolution have been obtained. These belonged to space group P212121, with unit-cell parameters a = 94.31, b = 125.6, c = 162.8Å. The self-rotation function and Matthews coefficient calculations are consistent with the presence of a nine-subunit oligomer in the asymmetric unit.

KW - bacteriophage G20C

KW - putative small terminase

KW - Thermus thermophilus

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

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

IS - 8

ER -

The putative small terminase from the thermophilic dsDNA bacteriophage G20C is a nine-subunit oligomer

Abstract

Keywords

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