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| | <StructureSection load='5k21' size='340' side='right'caption='[[5k21]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5k21' size='340' side='right'caption='[[5k21]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k21]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_fortuitum_subsp._fortuitum_atcc_6841 Mycobacterium fortuitum subsp. fortuitum atcc 6841]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K21 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K21 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k21]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_fortuitum_subsp._fortuitum_DSM_46621_=_ATCC_6841_=_JCM_6387 Mycolicibacterium fortuitum subsp. fortuitum DSM 46621 = ATCC 6841 = JCM 6387]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K21 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6QF:PHENAZIN-1-OL'>6QF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MFORT_14352 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1214102 Mycobacterium fortuitum subsp. fortuitum ATCC 6841])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6QF:PHENAZIN-1-OL'>6QF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=5k21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k21 OCA], [http://pdbe.org/5k21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k21 RCSB], [http://www.ebi.ac.uk/pdbsum/5k21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k21 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=5k21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k21 OCA], [https://pdbe.org/5k21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k21 RCSB], [https://www.ebi.ac.uk/pdbsum/5k21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k21 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/K0V2D8_MYCFO K0V2D8_MYCFO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mycobacterium fortuitum subsp. fortuitum atcc 6841]] | + | [[Category: Mycolicibacterium fortuitum subsp. fortuitum DSM 46621 = ATCC 6841 = JCM 6387]] |
| - | [[Category: Costa, K C]] | + | [[Category: Costa KC]] |
| - | [[Category: Glasser, N R]] | + | [[Category: Glasser NR]] |
| - | [[Category: Newman, D K]] | + | [[Category: Newman DK]] |
| - | [[Category: Demethylase phenazine]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
K0V2D8_MYCFO
Publication Abstract from PubMed
The opportunistic pathogen Pseudomonas aeruginosa produces colorful redox-active metabolites called phenazines, which underpin biofilm development, virulence, and clinical outcomes. Although phenazines exist in many forms, the best studied is pyocyanin. Here, we describe pyocyanin demethylase (PodA), a hitherto uncharacterized protein that oxidizes the pyocyanin methyl group to formaldehyde and reduces the pyrazine ring via an unusual tautomerizing demethylation reaction. Treatment with PodA disrupts P. aeruginosa biofilm formation similarly to DNase, suggesting interference with the pyocyanin-dependent release of extracellular DNA into the matrix. PodA-dependent pyocyanin demethylation also restricts established biofilm aggregate populations experiencing anoxic conditions. Together, these results show that modulating extracellular redox-active metabolites can influence the fitness of a biofilm-forming microorganism.
Pyocyanin degradation by a tautomerizing demethylase inhibits Pseudomonas aeruginosa biofilms.,Costa KC, Glasser NR, Conway SJ, Newman DK Science. 2017 Jan 13;355(6321):170-173. doi: 10.1126/science.aag3180. Epub 2016, Dec 8. PMID:27940577[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Costa KC, Glasser NR, Conway SJ, Newman DK. Pyocyanin degradation by a tautomerizing demethylase inhibits Pseudomonas aeruginosa biofilms. Science. 2017 Jan 13;355(6321):170-173. doi: 10.1126/science.aag3180. Epub 2016, Dec 8. PMID:27940577 doi:http://dx.doi.org/10.1126/science.aag3180
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