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The 1.58 A resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding.

ABSTRACT: DNA packaging in tailed bacteriophages and in evolutionarily related herpesviruses is controlled by a viral-encoded terminase. As in a number of other phages, in the Bacillus subtilis bacteriophages SF6 and SPP1 the terminase complex consists of two proteins: G1P and G2P. The crystal structure of the N-terminal DNA-binding domain of the bacteriophage SF6 small terminase subunit G1P is reported. Structural comparison with other DNA-binding proteins allows a general model for the interaction of G1P with the packaging-initiation site to be proposed.

SUBMITTER: Benini S

PROVIDER: S-EPMC3614160 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding.

Benini Stefano S Chechik Maria M Ortiz Lombardía Miguel M Polier Sigrun S Leech Andrew A Shevtsov Mikhail B MB Alonso Juan C JC

Acta crystallographica. Section F, Structural biology and crystallization communications 20130328 Pt 4

DNA packaging in tailed bacteriophages and in evolutionarily related herpesviruses is controlled by a viral-encoded terminase. As in a number of other phages, in the Bacillus subtilis bacteriophages SF6 and SPP1 the terminase complex consists of two proteins: G1P and G2P. The crystal structure of the N-terminal DNA-binding domain of the bacteriophage SF6 small terminase subunit G1P is reported. Structural comparison with other DNA-binding proteins allows a general model for the interaction of G1 ...[more]

PMID: 23545641

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