2CMP

crystal structure of the DNA binding domain of G1P SMALL TERMINASE SUBUNIT from bacteriophage SF6

Summary for 2CMP

• Entry DOI: 10.2210/pdb2cmp/pdb
• Descriptor: TERMINASE SMALL SUBUNIT (2 entities in total)
• Functional Keywords: sf6, dna packaging, viral protein
• Biological source: BACTERIOPHAGE SF6
• Total number of polymer chains: 1
• Total formula weight: 6959.96

Authors

Benini, S.,Chechik, M.,Ortiz-Lombardia, M.,Polier, S.,Shevtsov, M.B.,DeLuchi, D.,Alonso, J.C.,Antson, A.A. (deposition date: 2006-05-11, release date: 2007-05-15, Last modification date: 2024-05-08)

Primary citation

Benini, S.,Chechik, M.,Ortiz-Lombardia, M.,Polier, S.,Leech, A.,Shevtsov, M.B.,Alonso, J.C.
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, 69:376-, 2013

PubMed 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.

PubMed: 23545641
DOI: 10.1107/S1744309113004399

Experimental method

X-RAY DIFFRACTION (1.58 Å)