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| | ==Structure of phenazine antibiotic biosynthesis protein with substrate== | | ==Structure of phenazine antibiotic biosynthesis protein with substrate== |
| - | <StructureSection load='3l2k' size='340' side='right' caption='[[3l2k]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3l2k' size='340' side='right'caption='[[3l2k]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3l2k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_milletiae"_kawakami_and_yoshida_1920 "bacillus milletiae" kawakami and yoshida 1920]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L2K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3l2k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pantoea_agglomerans Pantoea agglomerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L2K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PXC:PHENAZINE-1,6-DICARBOXYLIC+ACID'>PXC</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hgu|3hgu]], [[3hgv|3hgv]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PXC:PHENAZINE-1,6-DICARBOXYLIC+ACID'>PXC</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ehpF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=549 "Bacillus milletiae" Kawakami and Yoshida 1920])</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=3l2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l2k OCA], [https://pdbe.org/3l2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l2k RCSB], [https://www.ebi.ac.uk/pdbsum/3l2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l2k 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=3l2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l2k OCA], [http://pdbe.org/3l2k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l2k RCSB], [http://www.ebi.ac.uk/pdbsum/3l2k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l2k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8GPH0_ENTAG Q8GPH0_ENTAG] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l2/3l2k_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l2/3l2k_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus milletiae kawakami and yoshida 1920]] | + | [[Category: Large Structures]] |
| - | [[Category: Atanasova, V]] | + | [[Category: Pantoea agglomerans]] |
| - | [[Category: Bera, A K]] | + | [[Category: Atanasova V]] |
| - | [[Category: Parsons, J F]] | + | [[Category: Bera AK]] |
| - | [[Category: Antibiotic]] | + | [[Category: Parsons JF]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Pdc]]
| + | |
| - | [[Category: Phenazine]]
| + | |
| Structural highlights
Function
Q8GPH0_ENTAG
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
The structure of EhpF, a 41 kDa protein that functions in the biosynthetic pathway leading to the broad-spectrum antimicrobial compound D-alanylgriseoluteic acid (AGA), is reported. A cluster of approximately 16 genes, including ehpF, located on a 200 kbp plasmid native to certain strains of Pantoea agglomerans encodes the proteins that are required for the conversion of chorismic acid to AGA. Phenazine-1,6-dicarboxylate has been identified as an intermediate in AGA biosynthesis and deletion of ehpF results in accumulation of this compound in vivo. The crystallographic data presented here reveal that EhpF is an atypical member of the acyl-CoA synthase or ANL superfamily of adenylating enzymes. These enzymes typically catalyze two-step reactions involving adenylation of a carboxylate substrate followed by transfer of the substrate from AMP to coenzyme A or another phosphopantetheine. EhpF is distinguished by the absence of the C-terminal domain that is characteristic of enzymes from this family and is involved in phosphopantetheine binding and in the second half of the canonical two-step reaction that is typically observed. Based on the structure of EhpF and a bioinformatic analysis, it is proposed that EhpF and EhpG convert phenazine-1,6-dicarboxylate to 6-formylphenazine-1-carboxylate via an adenylyl intermediate.
Structure of the D-alanylgriseoluteic acid biosynthetic protein EhpF, an atypical member of the ANL superfamily of adenylating enzymes.,Bera AK, Atanasova V, Gamage S, Robinson H, Parsons JF Acta Crystallogr D Biol Crystallogr. 2010 Jun;66(Pt 6):664-72. Epub 2010 May 15. PMID:20516619[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bera AK, Atanasova V, Gamage S, Robinson H, Parsons JF. Structure of the D-alanylgriseoluteic acid biosynthetic protein EhpF, an atypical member of the ANL superfamily of adenylating enzymes. Acta Crystallogr D Biol Crystallogr. 2010 Jun;66(Pt 6):664-72. Epub 2010 May 15. PMID:20516619 doi:10.1107/S0907444910008425
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