Structures of Lactococcal Phage p2 Baseplate Shed Light on a Novel Mechanism of Host Attachment and Activation in Siphoviridae

Structure of Lactococcal Phage P2 Baseplate and its Mechanism of Activation.

Lactococcal Bacteriophage P2 Receptor-Binding Protein Structure Suggests a Common Ancestor Gene with Bacterial and Mammalian Viruses.

4 MG/ML OF COMPLEX, 25% PEG 2000 MME, 0.1 M NA-HEPES PH 7.5.

STRUCTURE OF THE LACTOPHAGE P2 RECEPTOR BINDING PROTEIN INCOMPLEX WITH GLYCEROL

STRUCTURE OF LACTOCOCCAL BACTERIOPHAGE P2 RECEPTOR BINDING PROTEIN

STRUCTURE OF LACTOCOCCAL BACTERIOPHAGE P2 RECEPTOR BINDING PROTEIN IN COMPLEX WITH A LLAMA VHH DOMAIN

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

CHAINS P AND Q: PHAGE P2 SEQUENCE IS DEPOSITED IN GENBANK, NR GQ253898

THE BIOLOGICAL UNIT, THE BASEPLATE SHOULD BE RECONSTITUTED USING THE 3-FOLD CRYSTALLOGRAPHIC SYMMETRY
PUTATIVE RECEPTOR BINDING PROTEIN, CAMELID VHH5, LACTOCOCCAL PHAGE P2 ORF15, LACTOCOCCAL PHAGE P2 ORF16