2cmp

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

spinqualitylabelsall models 2cmp, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cmp is a 1 chain structure with sequence from Bpsf6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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