VtrA forms a complex with VtrC on the surface of the membrane that surrounds the bacterial cell. These two proteins create a platform that can bind to bile salts and trigger the release of bacterial toxins. This entry represents the C-terminal peripl ...
VtrA forms a complex with VtrC on the surface of the membrane that surrounds the bacterial cell. These two proteins create a platform that can bind to bile salts and trigger the release of bacterial toxins. This entry represents the C-terminal periplasmic domain of VtrA that interacts with the VtrC periplasmic domain. The VtrA periplasmic domain adopts an alpha/beta structure consisting of a five-stranded antiparallel beta-sheet and two helices packed on one side of it [1].
This entry represents a lipocalin-like beta barrel domain found in the Vibrio parahaemolyticus VtrC protein [1]. VtrC, along with VtrA and VtrB, are required for activating the virulence type III secretion system 2 in response to bile salts. The VtrA ...
This entry represents a lipocalin-like beta barrel domain found in the Vibrio parahaemolyticus VtrC protein [1]. VtrC, along with VtrA and VtrB, are required for activating the virulence type III secretion system 2 in response to bile salts. The VtrA/VtrC complex activates VtrB in the presence of bile salts. The crystal structure of the periplasmic domains of the VtrA/VtrC heterodimer reveals a beta-barrel with a hydrophobic inner chamber [1].