| the tailspike protein of shigella phage sf6. a structural homolog of salmonella phage p22 tailspike protein without sequence similarity in the beta-helix domain. | bacteriophage sf6 tailspike protein is functionally equivalent to the well characterized tailspike of salmonella phage p22, mediating attachment of the viral particle to host cell-surface polysaccharide. however, there is significant sequence similarity between the two 70-kda polypeptides only in the n-terminal putative capsid-binding domains. the major, central part of p22 tailspike protein, which forms a parallel beta-helix and is responsible for saccharide binding and hydrolysis, lacks detect ... | 2003 | 12424253 |
| complete genome sequence of phihsic, a pseudotemperate marine phage of listonella pelagia. | the genome for the marine pseudotemperate member of the siphoviridae phihsic has been sequenced using a combination of linker amplification library construction, restriction digest library construction, and primer walking. phihsic enters into a pseudolysogenic relationship with its host, listonella pelagia, characterized by sigmoidal growth curves producing >10(9) cells/ml and >10(11) phage/ml. the genome (37,966 bp; g+c content, 44%) contained 47 putative open reading frames (orfs), 17 of which ... | 2005 | 15933034 |
| an intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of shigella flexneri phage sf6. | sf6 belongs to the podoviridae family of temperate bacteriophages that infect gram-negative bacteria by insertion of their double-stranded dna. they attach to their hosts specifically via their tailspike proteins. the 1.25 a crystal structure of shigella phage sf6 tailspike protein (sf6 tsp) reveals a conserved architecture with a central, right-handed beta helix. in the trimer of sf6 tsp, the parallel beta helices form a left-handed, coiled-beta coil with a pitch of 340 a. the c-terminal domain ... | 2008 | 18462681 |
| crystal structure of escherichia coli phage hk620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related. | bacteriophage hk620 infects escherichia coli h and is closely related to shigella phage sf6 and salmonella phage p22. all three podoviridae recognize and cleave their respective host cell receptor polysaccharide by homotrimeric tailspike proteins. the three proteins exhibit high sequence identity in the 110 residues of their n-terminal particle-binding domains, but no apparent sequence similarity in their major, receptor-binding parts. we have biochemically characterized the receptor-binding par ... | 2008 | 18547389 |
| the host outer membrane proteins ompa and ompc are associated with the shigella phage sf6 virion. | assembly of dsdna bacteriophage is a precisely programmed process. potential roles of host cell components in phage assembly haven't been well understood. it was previously reported that two unidentified proteins were present in bacteriophage sf6 virion (casjens et al, 2004, j.mol.biol. 339, 379-394, fig. 2a). using tandem mass spectrometry, we have identified the two proteins as outer membrane proteins (omps) ompa and ompc from its host shigella flexneri. the transmission electron cryo-microsco ... | 2010 | 21071053 |