3sk2

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Current revision (09:51, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3sk2' size='340' side='right'caption='[[3sk2]], [[Resolution|resolution]] 1.01&Aring;' scene=''>
<StructureSection load='3sk2' size='340' side='right'caption='[[3sk2]], [[Resolution|resolution]] 1.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sk2]] is a 2 chain structure with sequence from [https://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=3SK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SK2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sk2]] 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=3SK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SK2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GRI:6-FORMYL-9-METHOXYPHENAZINE-1-CARBOXYLIC+ACID'>GRI</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.01&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ehpR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=549 "Bacillus milletiae" Kawakami and Yoshida 1920])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GRI:6-FORMYL-9-METHOXYPHENAZINE-1-CARBOXYLIC+ACID'>GRI</scene></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=3sk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sk2 OCA], [https://pdbe.org/3sk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sk2 RCSB], [https://www.ebi.ac.uk/pdbsum/3sk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sk2 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=3sk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sk2 OCA], [https://pdbe.org/3sk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sk2 RCSB], [https://www.ebi.ac.uk/pdbsum/3sk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sk2 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/EHPR_ENTAG EHPR_ENTAG] Required for resistance to the phenazine antibiotic D-alanylgriseoluteic acid (AGA), an antibiotic produced by E.agglomerans itself, and thus protects the bacterium against phenazine toxicity. Probably binds AGA and acts as a chaperone that works in tandem with a membrane transporter for subsequent antibiotic secretion.<ref>PMID:12139622</ref> <ref>PMID:21849072</ref>
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ABSTRACT: BACKGROUND: The phenazines are redox-active secondary metabolites that a large number of bacterial strains produce and excrete into the environment. They possess antibiotic activity owing to the fact that they can reduce molecular oxygen to toxic reactive oxygen species. In order to take advantage of this activity, phenazine producers need to protect themselves against phenazine toxicity. Whereas it is believed that phenazine-producing pseudomonads possess highly active superoxide dismutases and catalases, it has recently been found that the plant-colonizing bacterium Enterobacter agglomerans expresses a small gene ehpR to render itself resistant towards D-alanyl-griseoluteic acid, the phenazine antibiotic produced by this strain. RESULTS: To understand the resistance mechanism installed by EhpR we have determined its crystal structure in the apo form at 2.15 A resolution and in complex with griseoluteic acid at 1.01 A, respectively. While EhpR shares a common fold with glyoxalase-I / bleomycin resistance proteins, the ligand binding site does not contain residues that some related proteins employ to chemically alter their substrates. Binding of the antibiotic is mediated by pi-stacking interactions of the aromatic moiety with the side chains of aromatic amino acids and by a few polar interactions. The dissociation constant KD between EhpR and griseoluteic acid was quantified as 244 +/- 45 uM by microscale thermophoresis measurements. CONCLUSIONS: The data accumulated here suggest that EhpR confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. It is tempting to speculate that EhpR acts in concert with EhpJ, a transport protein of the major facilitator superfamily that is also encoded in the phenazine biosynthesis operon of E. agglomerans. The low affinity of EhpR for griseoluteic acid may be required for its physiological function.
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Atomic resolution structure of EhpR: phenazine resistance in Enterobacter agglomerans Eh1087 follows principles of bleomycin / mitomycin C resistance in other bacteria.,Yu S, Vit A, Devenish S, Mahanty HK, Itzen A, Goody RS, Blankenfeldt W BMC Struct Biol. 2011 Aug 17;11(1):33. PMID:21849072<ref>PMID:21849072</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3sk2" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus milletiae kawakami and yoshida 1920]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Blankenfeldt, W]]
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[[Category: Pantoea agglomerans]]
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[[Category: Yu, S]]
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[[Category: Blankenfeldt W]]
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[[Category: Antibiotic resistance]]
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[[Category: Yu S]]
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[[Category: Griseoluteate-binding protein]]
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Current revision

Crystal structure of phenazine resistance protein EhpR from Enterobacter agglomerans (Erwinia herbicola, Pantoea agglomerans) Eh1087 in complex with griseoluteic acid

PDB ID 3sk2

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