Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
The 1.58 A resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding.,Benini S, Chechik M, Ortiz Lombardia M, Polier S, Leech A, Shevtsov MB, Alonso JC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):376-81., doi: 10.1107/S1744309113004399. Epub 2013 Mar 28. PMID:23545641[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Benini S, Chechik M, Ortiz Lombardia M, Polier S, Leech A, Shevtsov MB, Alonso JC. The 1.58 A resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):376-81., doi: 10.1107/S1744309113004399. Epub 2013 Mar 28. PMID:23545641 doi:http://dx.doi.org/10.1107/S1744309113004399
