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2pbx

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{{STRUCTURE_2pbx| PDB=2pbx | SCENE= }}
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'''Vibrio cholerae HapR'''
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===Vibrio cholerae HapR===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Vibrio cholerae]]
[[Category: Vibrio cholerae]]
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Revision as of 12:43, 29 July 2008

Image:2pbx.png

Template:STRUCTURE 2pbx

Vibrio cholerae HapR

Template:ABSTRACT PUBMED 17526705

About this Structure

2PBX is a Single protein structure of sequence from Bacteria. 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

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