The 1.58 Å resolution structure of the DNA‐binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding. Issue 4 (2nd April 2013)

• Record Type: Journal Article
• Authors: Benini, Stefano; Chechik, Maria; Ortiz Lombardía, Miguel; Polier, Sigrun; Leech, Andrew; Shevtsov, Mikhail B.; Alonso, Juan C.
• Is Part Of: Acta crystallographica. Volume 69:Issue 4(2013:Apr.)
• Page Start: 376
• Page End: 381
• Publication Date: 2013-04-02
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113004399
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Bacillus subtilis</italic> 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.</p> </abstract>