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

DOI: 10.1107/S1744309113017016 DOI Help
PMID: 23908032 PMID Help

Authors: Juan Loredo-varela (University of York) , Maria Chechik (University of York) , Vladimir Levdikov (University of York) , Ahmad Abd-el-aziz (University of York) , Leonid Minakhin (The State University of New Jersey) , Konstantin Severinov (Rutgers, The State University of New Jersey; Institutes of Molecular Genetics and Gene Biology, Russian Academy of Sciences) , Callum Smits (University of York) , 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 , PAGES 876 - 879

State: Published (Approved)
Published: August 2013

Open Access Open Access

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 Å resolution have been obtained. These belonged to space group P212121, with unit-cell parameters a = 94.31, b = 125.6, c = 162.8 Å. The self-rotation function and Matthews coefficient calculations are consistent with the presence of a nine-subunit oligomer in the asymmetric unit.

Journal Keywords: The Assembly Of Double-Stranded Dna Bacteriophages Is Dependent On A Small

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography