@article {4928,
	title = {The binding of cholera toxin to the periplasmic vestibule of the type II secretion channel.},
	journal = {Channels},
	volume = {5},
	year = {2011},
	month = {2011 May-Jun},
	pages = {215-8},
	abstract = {<p>The type II secretion system (T2SS) is a large macromolecular complex spanning the inner and outer membranes of many gram-negative bacteria. The T2SS is responsible for the secretion of virulence factors such as cholera toxin (CT) and heat-labile enterotoxin (LT) from Vibrio cholerae and enterotoxigenic Escherichia coli, respectively. CT and LT are closely related AB5 heterohexamers, composed of one A subunit and a B-pentamer. Both CT and LT are translocated, as folded protein complexes, from the periplasm across the outer membrane through the type II secretion channel, the secretin GspD. We recently published the 19 {\r A} structure of the V. cholerae secretin (VcGspD) in its closed state and showed by SPR measurements that the periplasmic domain of GspD interacts with the B-pentamer complex. Here we extend these studies by characterizing the binding of the cholera toxin B-pentamer to VcGspD using electron microscopy of negatively stained preparations. Our studies indicate that the pentamer is captured within the large periplasmic vestibule of VcGspD. These new results agree well with our previously published studies and are in accord with a piston-driven type II secretion mechanism.</p>
},
	keywords = {Bacterial Proteins, Bacterial Secretion Systems, Cholera Toxin, Periplasm, Porins, Protein Folding, Protein Structure, Protein Subunits, Protein Transport, Quaternary, Tertiary, Vibrio cholerae},
	issn = {1933-6969},
	author = {Reichow, Steve L and Korotkov, Konstantin V and Gonen, Melissa and Sun, Ji and Delarosa, Jaclyn R and Hol, Wim G J and Gonen, Tamir}
}
@article {45965,
	title = {A conformational switch in bacteriophage p22 portal protein primes genome injection.},
	journal = {Molecular Cell},
	volume = {29},
	year = {2008},
	month = {2008 Feb 15},
	pages = {376-83},
	abstract = {<p>Double-stranded DNA (dsDNA) viruses such as herpesviruses and bacteriophages infect by delivering their genetic material into cells, a task mediated by a DNA channel called "portal protein." We have used electron cryomicroscopy to determine the structure of bacteriophage P22 portal protein in both the procapsid and mature capsid conformations. We find that, just as the viral capsid undergoes major conformational changes during virus maturation, the portal protein switches conformation from a procapsid to a mature phage state upon binding of gp4, the factor that initiates tail assembly. This dramatic conformational change traverses the entire length of the DNA channel, from the outside of the virus to the inner shell, and erects a large dome domain directly above the DNA channel that binds dsDNA inside the capsid. We hypothesize that this conformational change primes dsDNA for injection and directly couples completion of virus morphogenesis to a new cycle of infection.</p>
},
	keywords = {Bacteriophage P22, Binding Sites, Capsid Proteins, DNA, Viral, Genome, Models, Molecular, Protein Binding, Protein Conformation, Viral Tail Proteins},
	issn = {1097-2765},
	doi = {10.1016/j.molcel.2007.11.034},
	author = {Zheng, Hongjin and Olia, Adam S and Gonen, Melissa and Andrews, Simeon and Cingolani, Gino and Gonen, Tamir}
}
