CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEINCRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN
Structural highlights
1lkt is a 6 chain structure with sequence from Salmonella virus P22. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
FIBER_BPP22 Structural component of the short non-contractile tail. The tail comprises six fibers that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.[1][2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Weigele PR, Scanlon E, King J. Homotrimeric, beta-stranded viral adhesins and tail proteins. J Bacteriol. 2003 Jul;185(14):4022-30. PMID:12837775
↑Andres D, Hanke C, Baxa U, Seul A, Barbirz S, Seckler R. Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitro. J Biol Chem. 2010 Nov 19;285(47):36768-75. doi: 10.1074/jbc.M110.169003. Epub, 2010 Sep 3. PMID:20817910 doi:http://dx.doi.org/10.1074/jbc.M110.169003
