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Title: 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- Angstroms 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.

Authors:
; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
959601
Report Number(s):
BNL-82587-2009-JA
Journal ID: ISSN 0021-9193; JOBAAY; TRN: US201016%%745
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Bacteriology; Journal Volume: 189
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CRYSTAL STRUCTURE; DIMERIZATION; DNA; GENES; PHOSPHOTRANSFERASES; PROTEINS; RESIDUES; RESOLUTION; SOLVENTS; VIRULENCE; national synchrotron light source

Citation Formats

DeSilva,R., Kovacikova, G., Lin, W., Taylor, R., Skorupski, K., and Kull, F. Crystal Structure of the Vibrio Cholerae Quorum-Sensing Regulatory Protein HapR. United States: N. p., 2007. Web. doi:10.1128/JB.01807-06.
DeSilva,R., Kovacikova, G., Lin, W., Taylor, R., Skorupski, K., & Kull, F. Crystal Structure of the Vibrio Cholerae Quorum-Sensing Regulatory Protein HapR. United States. doi:10.1128/JB.01807-06.
DeSilva,R., Kovacikova, G., Lin, W., Taylor, R., Skorupski, K., and Kull, F. Mon . "Crystal Structure of the Vibrio Cholerae Quorum-Sensing Regulatory Protein HapR". United States. doi:10.1128/JB.01807-06.
@article{osti_959601,
title = {Crystal Structure of the Vibrio Cholerae Quorum-Sensing Regulatory Protein HapR},
author = {DeSilva,R. and Kovacikova, G. and Lin, W. and Taylor, R. and Skorupski, K. and Kull, F.},
abstractNote = {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- Angstroms 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.},
doi = {10.1128/JB.01807-06},
journal = {Journal of Bacteriology},
number = ,
volume = 189,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}