2pbx: Difference between revisions

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[[Image:2pbx.jpg|left|200px]]
[[Image:2pbx.jpg|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pbx OCA], [http://www.ebi.ac.uk/pdbsum/2pbx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pbx RCSB]</span>
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'''Vibrio cholerae HapR'''
'''Vibrio cholerae HapR'''
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[[Category: Skorupski, K.]]
[[Category: Skorupski, K.]]
[[Category: Taylor, R K.]]
[[Category: Taylor, R K.]]
[[Category: dna-binding]]
[[Category: Dna-binding]]
[[Category: protease]]
[[Category: Protease]]
[[Category: quorum sensing]]
[[Category: Quorum sensing]]
[[Category: tetr family]]
[[Category: Tetr family]]
[[Category: transcription factor]]
[[Category: Transcription factor]]
[[Category: transcription regulation]]
[[Category: Transcription regulation]]
[[Category: vibrio cholerae]]
[[Category: Vibrio cholerae]]
 
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Revision as of 12:48, 4 May 2008

File:2pbx.jpg

Template:STRUCTURE 2pbx

Vibrio cholerae HapR


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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 Sun May 4 12:48:31 2008

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