|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4za6' size='340' side='right'caption='[[4za6]], [[Resolution|resolution]] 1.97Å' scene=''> | | <StructureSection load='4za6' size='340' side='right'caption='[[4za6]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4za6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZA6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4za6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZA6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">QV65_28910 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 "Mycobacterium erythropolis" Gray and Thornton 1928])</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=4za6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4za6 OCA], [https://pdbe.org/4za6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4za6 RCSB], [https://www.ebi.ac.uk/pdbsum/4za6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4za6 ProSAT]</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=4za6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4za6 OCA], [http://pdbe.org/4za6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4za6 RCSB], [http://www.ebi.ac.uk/pdbsum/4za6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4za6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0C2W9F0_RHOER A0A0C2W9F0_RHOER] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Mycobacterium erythropolis gray and thornton 1928]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Morera, S]] | + | [[Category: Rhodococcus erythropolis]] |
| - | [[Category: Sahili, A El]] | + | [[Category: El Sahili A]] |
| - | [[Category: Nahl degradation]] | + | [[Category: Morera S]] |
| - | [[Category: Qsda transcriptional regulator]]
| + | |
| - | [[Category: Quorum-sensing]]
| + | |
| - | [[Category: Rhodococcus erythropolis r138]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
A0A0C2W9F0_RHOER
Publication Abstract from PubMed
Quorum-quenching (QQ) are natural or engineered processes disrupting the quorum-sensing (QS) signalling which controls virulence and persistence (e.g. biofilm) in numerous bacteria. QQ involves different enzymes including lactonases, amidases, oxidases and reductases which degrade the QS molecules such as N-acylhomoserine lactones (NAHL). Rhodococcus erythropolis known to efficiently degrade NAHL is proposed as a biocontrol agent and a reservoir of QQ-enzymes for biotechnology. In R. erythropolis, regulation of QQ-enzymes remains unclear. In this work, we performed genome engineering on R. erythropolis, which is recalcitrant to reverse genetics, in order to investigate regulation of QQ-enzymes at a molecular and structural level with the aim to improve the QQ activity. Deep-sequencing of the R. erythropolis enhanced variants allowed identification of a punctual mutation in a key-transcriptional factor QsdR (Quorum sensing degradation Regulation) which regulates the sole QQ-lactonase QsdA identified so far. Using biophysical and structural studies on QsdR, we demonstrate that QQ activity can be improved by modifying the regulation of QQ-enzymes degrading QS signal. This modification requiring the change of only one amino-acid in a transcriptional factor leads to an enhanced R. erythropolis in which the QS-signal degradation pathway is strongly activated.
Natural Guided Genome Engineering Reveals Transcriptional Regulators Controlling Quorum-Sensing Signal Degradation.,El Sahili A, Kwasiborski A, Mothe N, Velours C, Legrand P, Morera S, Faure D PLoS One. 2015 Nov 10;10(11):e0141718. doi: 10.1371/journal.pone.0141718., eCollection 2015. PMID:26554837[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ El Sahili A, Kwasiborski A, Mothe N, Velours C, Legrand P, Morera S, Faure D. Natural Guided Genome Engineering Reveals Transcriptional Regulators Controlling Quorum-Sensing Signal Degradation. PLoS One. 2015 Nov 10;10(11):e0141718. doi: 10.1371/journal.pone.0141718., eCollection 2015. PMID:26554837 doi:http://dx.doi.org/10.1371/journal.pone.0141718
|
