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Biol , Many Gram-negative bacteria use the multi-protein type II secretion system T2SS to selectively translocate virulence factors from the periplasmic space into the extracellular environment. In Vibrio cholerae the T2SS is called the extracellular protein secretion Eps system, which translocates cholera toxin and several enzymes in their folded state across the outer membrane.
We report here the 2. In a tentative model of a T2SS pseudopilus with EpsH at its tip, the conserved crevice faces away from the helix axis. This conserved surface region may be critical for interacting with other proteins from the T2SS machinery. Bioinformatics analyses suggested that PilZ domains bind c-di-GMP and allosterically modulate effector pathways.
We have determined a 1. Either this protein or another specific PilZ domain-containing protein is required for V. This switch brings the PilZ domain into close apposition with the N-terminal domain, forming a new allosteric interaction surface that spans these domains and the c-di-GMP at their interface. The very small size of the N-terminal conformational switch is likely to explain the facile evolutionary diversification of the PilZ domain.
Bussiere,3 Howard Robinson,4 and Michael A. The VC crystal structure has a few fungi and other eukaryotes. Although its molecular been determined at 2. Sequence conser- known to regulate changes in bacterial cell surfaces, as vation within the DUF84 and COG families was part of an adaptive response to promote bacterial persis- used to identify a conserved patch of surface resi- tence and proliferation.
VC, a conserved hypothetical protein of unknown function from Vibrio cholerae, resides in a three-gene operon containing the MbaA gene that encodes for a GGDEF and EAL domain-containing protein which is involved in regulating formation of the extracellular matrix of biofilms in Vibrio cholerae. The VC crystal structure has been determined at 2. Sequence conservation within the DUF84 and COG families was used to identify a conserved patch of surface residues that define a cleft and potential substrate-binding site in VC The three-dimensional structure of VC is similar to that of Mj from Methanococcus janeschii, which has been identified as a novel NTPase that binds NTP in a deep cleft similarly located to the conserved patch of surface residues that define an analogous cleft in VC Collectively, the data suggest that VC may have a biochemical function that involves NTP binding and phosphatase activity of some kind, and is likely involved in regulation of the signaling pathway that controls biofilm formation and maintenance in Vibrio cholerae.