2pbx

From Proteopedia

Revision as of 11:19, 23 January 2008

Vibrio cholerae HapR

Overview

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, gene expression and biofilm formation. The C-terminal dimerization domain, contains a unique solvent accessible tunnel connected to an amphipathic, cavity, which by analogy with other TetR regulators, may serve as a, binding pocket for an as-yet-unidentified ligand.

About this Structure

2PBX is a Single protein structure of sequence from Vibrio cholerae o1. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Vibrio cholerae quorum-sensing regulatory protein HapR., De Silva RS, Kovacikova G, Lin W, Taylor RK, Skorupski K, Kull FJ, J Bacteriol. 2007 Aug;189(15):5683-91. Epub 2007 May 25. PMID:17526705

Page seeded by OCA on Wed Jan 23 13:19:27 2008