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

Stefano Benini,Maria Chechik,Miguel Ortiz Lombardía,Sigrun Polier,Andrew Leech,Mikhail B Shevtsov,Juan C Alonso

Acta crystallographica. Section F, Structural biology and crystallization communications（2013）

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摘要

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.

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关键词

dna-binding domains,g1p,sf6,bacteriophages,terminases,viruses,sequence alignment,binding sites,dna binding domains,dna,amino acid sequence

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