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| | <StructureSection load='1ty9' size='340' side='right'caption='[[1ty9]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1ty9' size='340' side='right'caption='[[1ty9]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ty9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TY9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TY9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ty9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TY9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t9m|1t9m]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHZG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 "Bacillus fluorescens liquefaciens" Flugge 1886])</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=1ty9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ty9 OCA], [https://pdbe.org/1ty9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ty9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ty9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ty9 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ty9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ty9 OCA], [http://pdbe.org/1ty9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ty9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ty9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ty9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHZG_PSEFL PHZG_PSEFL]] Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control. Probably catalyzes the final step in the conversion of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) to phenazine-1-carboxylic acid (PCA). | + | [https://www.uniprot.org/uniprot/PHZG_PSEFL PHZG_PSEFL] Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control. Probably catalyzes the final step in the conversion of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) to phenazine-1-carboxylic acid (PCA). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens liquefaciens flugge 1886]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Eisenstein, E]] | + | [[Category: Pseudomonas fluorescens]] |
| - | [[Category: Ladner, J E]] | + | [[Category: Eisenstein E]] |
| - | [[Category: Parsons, J F]] | + | [[Category: Ladner JE]] |
| - | [[Category: Chorismate]] | + | [[Category: Parsons JF]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Phenazine]]
| + | |
| - | [[Category: Phzg]]
| + | |
| - | [[Category: Pseudomona]]
| + | |
| Structural highlights
Function
PHZG_PSEFL Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control. Probably catalyzes the final step in the conversion of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) to phenazine-1-carboxylic acid (PCA).
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
PhzG is a flavin-dependent oxidase that is believed to play a role in phenazine antibiotic synthesis in various bacteria, including Pseudomonas. Phenazines are chorismic acid derivatives that provide the producing organisms, including the opportunistic pathogen P. aeruginosa, with a competitive growth advantage. Here, the crystal structures of PhzG from both P. aeruginosa and P. fluorescens solved in an unliganded state at 1.9 and 1.8 A resolution, respectively, are described. Although the specific reaction in phenazine biosynthesis catalyzed by PhzG is unknown, the structural data indicates that PhzG is closely related to pyridoxine-5'-phosphate oxidase, the Escherichia coli pdxH gene product, which catalyzes the final step in pyridoxal-5'-phosphate (PLP) biosynthesis. A previous proposal suggested that the physiological substrate of PhzG to be 2,3-dihydro-3-hydroxyanthranilic acid (DHHA), a phenazine precursor produced by the sequential actions of the PhzE and PhzD enzymes on chorismate, and that two DHHA molecules dimerized in another enzyme-catalyzed reaction to yield phenazine-1-carboxylate. However, it was not possible to demonstrate any in vitro activity upon incubation of PhzG and DHHA. Interestingly, analysis of the in vitro activities of PhzG in combination with PhzF suggests that PhzF acts on DHHA and that PhzG then reacts with a non-aromatic tricyclic phenazine precusor to catalyze an oxidation/aromatization reaction that yields phenazine-1-carboxylate. It is proposed that phzG arose by duplication of pdxH and that the subtle differences seen between the structures of PhzG and PdxH correlate with the loss of the ability of PhzG to catalyze PLP formation. Sequence alignments and superimpositions of the active sites of PhzG and PdxH reveal that the residues that form a positively charged pocket around the phosphate of PLP in the PdxH-PLP complex are not conserved in PhzG, consistent with the inability of phosphorylated compounds to serve as substrates for PhzG.
Structure of the phenazine biosynthesis enzyme PhzG.,Parsons JF, Calabrese K, Eisenstein E, Ladner JE Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):2110-3. Epub 2004, Oct 20. PMID:15502343[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Parsons JF, Calabrese K, Eisenstein E, Ladner JE. Structure of the phenazine biosynthesis enzyme PhzG. Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):2110-3. Epub 2004, Oct 20. PMID:15502343 doi:10.1107/S0907444904022474
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