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| | <StructureSection load='5buf' size='340' side='right'caption='[[5buf]], [[Resolution|resolution]] 2.37Å' scene=''> | | <StructureSection load='5buf' size='340' side='right'caption='[[5buf]], [[Resolution|resolution]] 2.37Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5buf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acib3 Acib3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BUF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BUF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5buf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_AB307-0294 Acinetobacter baumannii AB307-0294]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BUF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.37Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABBFA_001168 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=557600 ACIB3])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-phosphoshikimate_1-carboxyvinyltransferase 3-phosphoshikimate 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.19 2.5.1.19] </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=5buf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5buf OCA], [https://pdbe.org/5buf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5buf RCSB], [https://www.ebi.ac.uk/pdbsum/5buf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5buf 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=5buf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5buf OCA], [http://pdbe.org/5buf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5buf RCSB], [http://www.ebi.ac.uk/pdbsum/5buf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5buf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Function == | |
| - | [[http://www.uniprot.org/uniprot/A0A0A7XPK6_ACIBA A0A0A7XPK6_ACIBA]] Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.[SAAS:SAAS00240586] | |
| | <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 5buf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5buf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[EPSP synthase 3D structures|EPSP synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-phosphoshikimate 1-carboxyvinyltransferase]] | + | [[Category: Acinetobacter baumannii AB307-0294]] |
| - | [[Category: Acib3]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Breen, J]] | + | [[Category: Breen J]] |
| - | [[Category: Graham, J]] | + | [[Category: Graham J]] |
| - | [[Category: Schultz, L W]] | + | [[Category: Schultz LW]] |
| - | [[Category: Sutton, K A]] | + | [[Category: Sutton KA]] |
| - | [[Category: Umland, T C]] | + | [[Category: Umland TC]] |
| - | [[Category: Epsp synthase]]
| + | |
| - | [[Category: Shikimate pathway]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the sixth step of the seven-step shikimate pathway. Chorismate, the product of the pathway, is a precursor for the biosynthesis of aromatic amino acids, siderophores and metabolites such as folate, ubiquinone and vitamin K. The shikimate pathway is present in bacteria, fungi, algae, plants and apicomplexan parasites, but is absent in humans. The EPSP synthase enzyme produces 5-enolpyruvylshikimate 3-phosphate and phosphate from phosphoenolpyruvate and shikimate 3-phosphate via a transferase reaction, and is the target of the herbicide glyphosate. The Acinetobacter baumannii gene encoding EPSP synthase, aroA, has previously been demonstrated to be essential during host infection for the growth and survival of this clinically important drug-resistant ESKAPE pathogen. Prephenate dehydrogenase is also encoded by the bifunctional A. baumannii aroA gene, but its activity is dependent upon EPSP synthase since it operates downstream of the shikimate pathway. As part of an effort to evaluate new antimicrobial targets, recombinant A. baumannii EPSP (AbEPSP) synthase, comprising residues Ala301-Gln756 of the aroA gene product, was overexpressed in Escherichia coli, purified and crystallized. The crystal structure, determined to 2.37 A resolution, is described in the context of a potential antimicrobial target and in comparison to EPSP synthases that are resistant or sensitive to the herbicide glyphosate.
Crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the ESKAPE pathogen Acinetobacter baumannii.,Sutton KA, Breen J, Russo TA, Schultz LW, Umland TC Acta Crystallogr F Struct Biol Commun. 2016 Mar 1;72(Pt 3):179-87. doi:, 10.1107/S2053230X16001114. Epub 2016 Feb 16. PMID:26919521[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sutton KA, Breen J, Russo TA, Schultz LW, Umland TC. Crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the ESKAPE pathogen Acinetobacter baumannii. Acta Crystallogr F Struct Biol Commun. 2016 Mar 1;72(Pt 3):179-87. doi:, 10.1107/S2053230X16001114. Epub 2016 Feb 16. PMID:26919521 doi:http://dx.doi.org/10.1107/S2053230X16001114
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