2pbx
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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==About this Structure== | ==About this Structure== | ||
| - | 2PBX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 2PBX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PBX OCA]. |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/17526705 17526705] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17526705 17526705] | ||
| + | [[Category: Bacteria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Vibrio cholerae o1]] | ||
[[Category: DeSilva, R S.]] | [[Category: DeSilva, R S.]] | ||
[[Category: Kovacikova, G.]] | [[Category: Kovacikova, G.]] | ||
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[[Category: vibrio cholerae]] | [[Category: vibrio cholerae]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:34:00 2008'' |
Revision as of 01:34, 31 March 2008
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| , resolution 2.2Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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
Page seeded by OCA on Mon Mar 31 04:34:00 2008
