2wc9
CRYSTAL STRUCTURE OF THE G2P (LARGE TERMINASE) NUCLEASE DOMAIN FROM THE BACTERIOPHAGE SPP1 WITH BOUND MNCRYSTAL STRUCTURE OF THE G2P (LARGE TERMINASE) NUCLEASE DOMAIN FROM THE BACTERIOPHAGE SPP1 WITH BOUND MN
Template:ABSTRACT PUBMED 19444313
FunctionFunction
[TERL_BPSPP] Component of the molecular motor that translocates genomic DNA in empty capsid during DNA packaging. Heterodimerizes with small terminase protein to be docked on capsid portal protein. The latter forms a ring in which genomic DNA in translocated into the capsid. May have or induce an endonuclease activity to cleave the genome concatemer after encapsidation (By similarity).
About this StructureAbout this Structure
2wc9 is a 1 chain structure with sequence from Bacillus phage spp1. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Smits C, Chechik M, Kovalevskiy OV, Shevtsov MB, Foster AW, Alonso JC, Antson AA. Structural basis for the nuclease activity of a bacteriophage large terminase. EMBO Rep. 2009 Jun;10(6):592-8. Epub 2009 May 15. PMID:19444313 doi:10.1038/embor.2009.53