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2uxh

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Revision as of 02:27, 8 February 2016

TTGR IN COMPLEX WITH QUERCETIN

Structural highlights

2uxh is a 2 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2uxi
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TTGR_PSEPT] Represses expression from the ttgABC operon promoter and its own expression. Binds to a promoter region between the divergently transcribed ttgR and ttgABC genes/operons; in the presence of chloramphenicol or tetracycline this binding no longer occurs and ttgR and ttgABC are derepressed. This suggests that TtgR binds these antibiotics.^[1]

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

Antibiotic resistance is a widely spread phenomenon. One major mechanism that underlies antibiotic resistance in bacteria is the active extrusion of toxic compounds through the membrane-bound efflux pumps that are often regulated at the transcriptional level. TtgR represses the transcription of TtgABC, a key efflux pump in Pseudomonas putida, which is highly resistant to antibiotics, solvents and toxic plant secondary products. Previously we showed that TtgR is the only reported repressor that binds to different classes of natural antimicrobial compounds, which are also extruded by the efflux pump. We report here five high-resolution crystal structures of TtgR from the solvent-tolerant strain DOT-T1E, including TtgR in complex with common antibiotics and plant secondary metabolites. We provide structural basis for the unique ligand binding properties of TtgR. We identify two distinct and overlapping ligand binding sites; the first one is broader and consists of mainly hydrophobic residues, whereas the second one is deeper and contains more polar residues including Arg176, a unique residue present in the DOT-T1E strain but not in other Pseudomonas strains. Phloretin, a plant antimicrobial, can bind to both binding sites with distinct binding affinities and stoichiometries. Results on ligand binding properties of native and mutant TtgR proteins using isothermal titration calorimetry confirm the binding affinities and stoichiometries, and suggest a potential positive cooperativity between the two binding sites. The importance of Arg176 in phloretin binding was further confirmed by the reduced ability of phloretin in releasing the mutant TtgR from bound DNA compared to the native protein. The results presented here highlight the importance and versatility of regulatory systems in bacterial antibiotic resistance and open up new avenues for novel antimicrobial development.

Crystal structures of multidrug binding protein TtgR in complex with antibiotics and plant antimicrobials.,Alguel Y, Meng C, Teran W, Krell T, Ramos JL, Gallegos MT, Zhang X J Mol Biol. 2007 Jun 8;369(3):829-40. Epub 2007 Mar 30. PMID:17466326^[2]

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

References

↑ Duque E, Segura A, Mosqueda G, Ramos JL. Global and cognate regulators control the expression of the organic solvent efflux pumps TtgABC and TtgDEF of Pseudomonas putida. Mol Microbiol. 2001 Feb;39(4):1100-6. PMID:11251828
↑ Alguel Y, Meng C, Teran W, Krell T, Ramos JL, Gallegos MT, Zhang X. Crystal structures of multidrug binding protein TtgR in complex with antibiotics and plant antimicrobials. J Mol Biol. 2007 Jun 8;369(3):829-40. Epub 2007 Mar 30. PMID:17466326 doi:http://dx.doi.org/S0022-2836(07)00428-7

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/2uxh"

@@ Line 2: / Line 2: @@
 <StructureSection load='2uxh' size='340' side='right' caption='[[2uxh]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2uxh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UXH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2uxh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UXH FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QUE:3,5,7,3,4-PENTAHYDROXYFLAVONE'>QUE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2uxi|2uxi]]</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=2uxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uxh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2uxh RCSB], [http://www.ebi.ac.uk/pdbsum/2uxh PDBsum]</span></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=2uxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uxh OCA], [http://pdbe.org/2uxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uxh RCSB], [http://www.ebi.ac.uk/pdbsum/2uxh PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TTGR_PSEPU TTGR_PSEPU]] Represses expression from the ttgABC operon promoter and its own expression. Binds to a promoter region between the divergently transcribed ttgR and ttgABC genes/operons; in the presence of chloramphenicol or tetracycline this binding no longer occurs and ttgR and ttgABC are derepressed. This suggests that TtgR binds these antibiotics.<ref>PMID:11251828</ref>
+[[http://www.uniprot.org/uniprot/TTGR_PSEPT TTGR_PSEPT]] Represses expression from the ttgABC operon promoter and its own expression. Binds to a promoter region between the divergently transcribed ttgR and ttgABC genes/operons; in the presence of chloramphenicol or tetracycline this binding no longer occurs and ttgR and ttgABC are derepressed. This suggests that TtgR binds these antibiotics.<ref>PMID:11251828</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2uxh ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2uxh" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Pseudomonas putida]]
+[[Category: Bacillus fluorescens putidus flugge 1886]]
 [[Category: Alguel, Y]]
 [[Category: Gallegos, M T]]

2uxh

From Proteopedia

Revision as of 02:27, 8 February 2016

TTGR IN COMPLEX WITH QUERCETIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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