2q0o
From Proteopedia
(New page: 200px<br /><applet load="2q0o" size="350" color="white" frame="true" align="right" spinBox="true" caption="2q0o, resolution 2.00Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Bacteria can communicate via diffusible signal molecules they generate and | + | Bacteria can communicate via diffusible signal molecules they generate and release to coordinate their behavior in response to the environment. Signal molecule concentration is often proportional to bacterial population density, and when this reaches a critical concentration, reflecting a bacterial quorum, specific behaviors including virulence, symbiosis, and horizontal gene transfer are activated. Quorum-sensing regulation in many Gram-negative bacteria involves acylated homoserine lactone signals that are perceived through binding to LuxR-type, acylated-homoserine-lactone-responsive transcription factors. Bacteria of the rhizobial group employ the LuxR-type transcriptional activator TraR in quorum sensing, and its activity is further regulated through interactions with the TraM antiactivator. In this study, we have crystallographically determined the 3D structure of the TraR-TraM antiactivation complex from Rhizobium sp. strain NGR234. Unexpectedly, the antiactivator TraM binds to TraR at a site distinct from its DNA-binding motif and induces an allosteric conformational change in the protein, thereby preventing DNA binding. Structural analysis reveals a highly conserved TraR-TraM interface and suggests a mechanism for antiactivation complex formation. This structure may inform alternative strategies to control quorum-sensing-regulated microbial activity including amelioration of infectious disease and antibiotic resistance. In addition, the structural basis of antiactivation presents a regulatory interaction that provides general insights relevant to the field of transcription regulation and signal transduction. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
[[Category: Fuqua, C.]] | [[Category: Fuqua, C.]] | ||
| - | [[Category: Jeffrey, P | + | [[Category: Jeffrey, P D.]] |
[[Category: Shi, Y.]] | [[Category: Shi, Y.]] | ||
[[Category: LAE]] | [[Category: LAE]] | ||
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[[Category: two-helix coiled coil]] | [[Category: two-helix coiled coil]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:34:50 2008'' |
Revision as of 16:34, 21 February 2008
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Crystal structure of an anti-activation complex in bacterial quorum sensing
Overview
Bacteria can communicate via diffusible signal molecules they generate and release to coordinate their behavior in response to the environment. Signal molecule concentration is often proportional to bacterial population density, and when this reaches a critical concentration, reflecting a bacterial quorum, specific behaviors including virulence, symbiosis, and horizontal gene transfer are activated. Quorum-sensing regulation in many Gram-negative bacteria involves acylated homoserine lactone signals that are perceived through binding to LuxR-type, acylated-homoserine-lactone-responsive transcription factors. Bacteria of the rhizobial group employ the LuxR-type transcriptional activator TraR in quorum sensing, and its activity is further regulated through interactions with the TraM antiactivator. In this study, we have crystallographically determined the 3D structure of the TraR-TraM antiactivation complex from Rhizobium sp. strain NGR234. Unexpectedly, the antiactivator TraM binds to TraR at a site distinct from its DNA-binding motif and induces an allosteric conformational change in the protein, thereby preventing DNA binding. Structural analysis reveals a highly conserved TraR-TraM interface and suggests a mechanism for antiactivation complex formation. This structure may inform alternative strategies to control quorum-sensing-regulated microbial activity including amelioration of infectious disease and antibiotic resistance. In addition, the structural basis of antiactivation presents a regulatory interaction that provides general insights relevant to the field of transcription regulation and signal transduction.
About this Structure
2Q0O is a Protein complex structure of sequences from Rhizobium sp. with as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for antiactivation in bacterial quorum sensing., Chen G, Jeffrey PD, Fuqua C, Shi Y, Chen L, Proc Natl Acad Sci U S A. 2007 Oct 16;104(42):16474-9. Epub 2007 Oct 5. PMID:17921255
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