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2q0o

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Revision as of 08:04, 25 June 2021

Crystal structure of an anti-activation complex in bacterial quorum sensing

Structural highlights

2q0o is a 4 chain structure with sequence from Ensifer fredii ngr234. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	traR (Ensifer fredii NGR234), traM (Ensifer fredii NGR234)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRAR_RHISN] Positive regulation of conjugal transfer. TraR activates target genes in the presence of AAI and also activates traR and traI themselves (By similarity). [TRAM_RHISN] Acts to antagonize TraR-dependent activation (Potential).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chen G, Jeffrey PD, Fuqua C, Shi Y, Chen L. Structural basis for antiactivation in bacterial quorum sensing. Proc Natl Acad Sci U S A. 2007 Oct 16;104(42):16474-9. Epub 2007 Oct 5. PMID:17921255

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2q0o"

@@ Line 1: / Line 1: @@
 ==Crystal structure of an anti-activation complex in bacterial quorum sensing==
-<StructureSection load='2q0o' size='340' side='right' caption='[[2q0o]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='2q0o' size='340' side='right'caption='[[2q0o]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2q0o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ensifer_fredii_ngr234 Ensifer fredii ngr234]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Q0O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2q0o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ensifer_fredii_ngr234 Ensifer fredii ngr234]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q0O FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAE:3-OXO-OCTANOIC+ACID+(2-OXO-TETRAHYDRO-FURAN-3-YL)-AMIDE'>LAE</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LAE:3-OXO-OCTANOIC+ACID+(2-OXO-TETRAHYDRO-FURAN-3-YL)-AMIDE'>LAE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">traR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=394 Ensifer fredii NGR234]), traM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=394 Ensifer fredii NGR234])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">traR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=394 Ensifer fredii NGR234]), traM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=394 Ensifer fredii NGR234])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q0o OCA], [http://pdbe.org/2q0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q0o RCSB], [http://www.ebi.ac.uk/pdbsum/2q0o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q0o ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q0o OCA], [https://pdbe.org/2q0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q0o RCSB], [https://www.ebi.ac.uk/pdbsum/2q0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q0o ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TRAR_RHISN TRAR_RHISN]] Positive regulation of conjugal transfer. TraR activates target genes in the presence of AAI and also activates traR and traI themselves (By similarity). [[http://www.uniprot.org/uniprot/TRAM_RHISN TRAM_RHISN]] Acts to antagonize TraR-dependent activation (Potential).
+[[https://www.uniprot.org/uniprot/TRAR_RHISN TRAR_RHISN]] Positive regulation of conjugal transfer. TraR activates target genes in the presence of AAI and also activates traR and traI themselves (By similarity). [[https://www.uniprot.org/uniprot/TRAM_RHISN TRAM_RHISN]] Acts to antagonize TraR-dependent activation (Potential).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 34: @@
 </StructureSection>
 [[Category: Ensifer fredii ngr234]]
+[[Category: Large Structures]]
 [[Category: Chen, G]]
 [[Category: Chen, L]]

2q0o

From Proteopedia

Revision as of 08:04, 25 June 2021

Crystal structure of an anti-activation complex in bacterial quorum sensing

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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