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| | <StructureSection load='4hmw' size='340' side='right'caption='[[4hmw]], [[Resolution|resolution]] 1.53Å' scene=''> | | <StructureSection load='4hmw' size='340' side='right'caption='[[4hmw]], [[Resolution|resolution]] 1.53Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hmw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HMW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HMW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hmw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_lata Burkholderia lata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HMW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | + | </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></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hms|4hms]], [[4hmt|4hmt]], [[4hmu|4hmu]], [[4hmv|4hmv]], [[4hmx|4hmx]]</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=4hmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hmw OCA], [https://pdbe.org/4hmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hmw RCSB], [https://www.ebi.ac.uk/pdbsum/4hmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hmw ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyridoxal_5'-phosphate_synthase Pyridoxal 5'-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.5 1.4.3.5] </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=4hmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hmw OCA], [http://pdbe.org/4hmw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hmw RCSB], [http://www.ebi.ac.uk/pdbsum/4hmw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hmw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PHZG_BURL3 PHZG_BURL3] Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control (PubMed:23897464). Catalyzes several oxidations in the terminal steps of core phenazine biosynthesis. It oxidizes both hexahydrophenazine-1,6-dicarboxylic acid (HHPDC) and tetrahydrophenazine-1-carboxylic acid (THPCA) and thereby contributes to the generation of both phenazine-1,6-dicarboxylic acid (PDC) and phenazine-1-carboxylic acid (PCA). It synthesizes phenazines in their reduced form, which are the likely end products in vivo (PubMed:23897464).<ref>PMID:23897464</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4hmw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4hmw" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Pyridoxine 5'-phosphate oxidase|Pyridoxine 5'-phosphate oxidase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Burkholderia lata]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pyridoxal 5'-phosphate synthase]]
| + | [[Category: Ahuja EG]] |
| - | [[Category: Ahuja, E G]] | + | [[Category: Blankenfeldt W]] |
| - | [[Category: Blankenfeldt, W]] | + | [[Category: Xu NN]] |
| - | [[Category: Xu, N N]] | + | |
| - | [[Category: Apo structure]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
PHZG_BURL3 Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control (PubMed:23897464). Catalyzes several oxidations in the terminal steps of core phenazine biosynthesis. It oxidizes both hexahydrophenazine-1,6-dicarboxylic acid (HHPDC) and tetrahydrophenazine-1-carboxylic acid (THPCA) and thereby contributes to the generation of both phenazine-1,6-dicarboxylic acid (PDC) and phenazine-1-carboxylic acid (PCA). It synthesizes phenazines in their reduced form, which are the likely end products in vivo (PubMed:23897464).[1]
Publication Abstract from PubMed
Phenazines are redox-active secondary metabolites that many bacteria produce and secrete into the environment. They are broad-specificity antibiotics, but also act as virulence and survival factors in infectious diseases. Phenazines are derived from chorismic acid, but important details of their biosynthesis are still unclear. For example, three two-electron oxidations seem to be necessary in the final steps of the pathway, while only one oxidase, the FMN-dependent PhzG, is conserved in the phenazine-biosynthesis phz operon. Here, crystal structures of PhzG from Pseudomonas fluorescens 2-79 and from Burkholderia lata 383 in complex with excess FMN and with the phenazine-biosynthesis intermediates hexahydrophenazine-1,6-dicarboxylate and tetrahydrophenazine-1-carboxylate generated in situ are reported. Corroborated with biochemical data, these complexes demonstrate that PhzG is the terminal enzyme in phenazine biosynthesis and that its relaxed substrate specificity lets it participate in the generation of both phenazine-1,6-dicarboxylic acid (PDC) and phenazine-1-carboxylic acid (PCA). This suggests that competition between flavin-dependent oxidations through PhzG and spontaneous oxidative decarboxylations determines the ratio of PDC, PCA and unsubstituted phenazine as the products of phenazine biosynthesis. Further, the results indicate that PhzG synthesizes phenazines in their reduced form. These reduced molecules, and not the fully aromatized derivatives, are the likely end products in vivo, explaining why only one oxidase is required in the phenazine-biosynthesis pathway.
Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis.,Xu N, Ahuja EG, Janning P, Mavrodi DV, Thomashow LS, Blankenfeldt W Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1403-13. doi:, 10.1107/S0907444913008354. Epub 2013 Jul 13. PMID:23897464[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xu N, Ahuja EG, Janning P, Mavrodi DV, Thomashow LS, Blankenfeldt W. Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis. Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1403-13. doi:, 10.1107/S0907444913008354. Epub 2013 Jul 13. PMID:23897464 doi:http://dx.doi.org/10.1107/S0907444913008354
- ↑ Xu N, Ahuja EG, Janning P, Mavrodi DV, Thomashow LS, Blankenfeldt W. Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis. Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1403-13. doi:, 10.1107/S0907444913008354. Epub 2013 Jul 13. PMID:23897464 doi:http://dx.doi.org/10.1107/S0907444913008354
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