Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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
