Crystal structure of the Vibrio cholerae quorum-sensing regulatory protein HapR.

ABSTRACT: Quorum sensing in Vibrio cholerae involves signaling between two-component sensor protein kinases and the response regulator LuxO to control the expression of the master regulator HapR. HapR, in turn, plays a central role in regulating a number of important processes, such as virulence gene expression and biofilm formation. We have determined the crystal structure of HapR to 2.2-A resolution. Its structure reveals a dimeric, two-domain molecule with an all-helical structure that is strongly conserved with members of the TetR family of transcriptional regulators. The N-terminal DNA-binding domain contains a helix-turn-helix DNA-binding motif and alteration of certain residues in this domain completely abolishes the ability of HapR to bind to DNA, alleviating repression of both virulence gen

SUBMITTER: De Silva RS 

PROVIDER: S-EPMC1951804 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature