@article {4926,
	title = {Secretins: dynamic channels for protein transport across membranes.},
	journal = {Trends in Biochemical Sciences},
	volume = {36},
	year = {2011},
	month = {2011 Aug},
	pages = {433-43},
	abstract = {<p>Secretins form megadalton bacterial-membrane channels in at least four sophisticated multiprotein systems that are crucial for translocation of proteins and assembled fibers across the outer membrane of many species of bacteria. Secretin subunits contain multiple domains, which interact with numerous other proteins, including pilotins, secretion-system partner proteins, and exoproteins. Our understanding of the structure of secretins is rapidly progressing, and it is now recognized that features common to all secretins include a cylindrical arrangement of 12-15 subunits, a large periplasmic vestibule with a wide opening at one end and a periplasmic gate at the other. Secretins might also play a key role in the biogenesis of their cognate secretion systems.</p>
},
	keywords = {Bacterial Outer Membrane Proteins, Bacterial Proteins, Carrier Proteins, Gram-Negative Bacteria, Membrane Transport Proteins, Models, Molecular, Protein Binding, Protein Conformation, Protein Structure, Protein Transport, Secondary, Secretin, Tertiary},
	issn = {0968-0004},
	doi = {10.1016/j.tibs.2011.04.002},
	author = {Korotkov, Konstantin V and Gonen, Tamir and Hol, Wim G J}
}
