The 1.58 Å 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
; 69(Pt 4): 376-81, 2013 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-23545641
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.
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1
Base de dados:
MEDLINE
Assunto principal:
DNA
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Fagos Bacilares
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Adenosina Trifosfatases
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Endodesoxirribonucleases
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Domínios e Motivos de Interação entre Proteínas
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Conformação de Ácido Nucleico
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Itália