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| | ==Structure of wild type Pseudomonas aeruginosa FabF (KASII) in Complex with ligand== | | ==Structure of wild type Pseudomonas aeruginosa FabF (KASII) in Complex with ligand== |
| - | <StructureSection load='4jpf' size='340' side='right' caption='[[4jpf]], [[Resolution|resolution]] 1.67Å' scene=''> | + | <StructureSection load='4jpf' size='340' side='right'caption='[[4jpf]], [[Resolution|resolution]] 1.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jpf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JPF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JPF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jpf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JPF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1LR:3-(BENZOYLAMINO)-2-HYDROXYBENZOIC+ACID'>1LR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.67Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b7v|4b7v]], [[4jb6|4jb6]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1LR:3-(BENZOYLAMINO)-2-HYDROXYBENZOIC+ACID'>1LR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FabF, fabF1, PA2965 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=4jpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpf OCA], [https://pdbe.org/4jpf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jpf RCSB], [https://www.ebi.ac.uk/pdbsum/4jpf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpf 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/Beta-ketoacyl-[acyl-carrier-protein]_synthase_II Beta-ketoacyl-[acyl-carrier-protein] synthase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.179 2.3.1.179] </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=4jpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpf OCA], [http://pdbe.org/4jpf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jpf RCSB], [http://www.ebi.ac.uk/pdbsum/4jpf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G3XDA2_PSEAE G3XDA2_PSEAE]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP (By similarity).[PIRNR:PIRNR000447] | + | [https://www.uniprot.org/uniprot/G3XDA2_PSEAE G3XDA2_PSEAE] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP (By similarity).[PIRNR:PIRNR000447] |
| | <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 4jpf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4jpf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pseae]] | + | [[Category: Large Structures]] |
| - | [[Category: Baum, B]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Brenk, R]] | + | [[Category: Baum B]] |
| - | [[Category: Jaenicke, E]] | + | [[Category: Brenk R]] |
| - | [[Category: Fabf]] | + | [[Category: Jaenicke E]] |
| - | [[Category: Fatty acid biosynthesis]]
| + | |
| - | [[Category: Kasii]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
G3XDA2_PSEAE Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP (By similarity).[PIRNR:PIRNR000447]
Publication Abstract from PubMed
Bacterial infections remain a serious health concern, in particular causing life-threatening infections of hospitalized and immunocompromised patients. The situation is exacerbated by the rise in antibacterial drug resistance, and new treatments are urgently sought. In this endeavour, accurate structures of molecular targets can support early-stage drug discovery. Here, crystal structures, in three distinct forms, of recombinant Pseudomonas aeruginosa beta-ketoacyl-(acyl-carrier-protein) synthase II (FabF) are presented. This enzyme, which is involved in fatty-acid biosynthesis, has been validated by genetic and chemical means as an antibiotic target in Gram-positive bacteria and represents a potential target in Gram-negative bacteria. The structures of apo FabF, of a C164Q mutant in which the binding site is altered to resemble the substrate-bound state and of a complex with 3-(benzoylamino)-2-hydroxybenzoic acid are reported. This compound mimics aspects of a known natural product inhibitor, platensimycin, and surprisingly was observed binding outside the active site, interacting with a symmetry-related molecule. An unusual feature is a completely buried potassium-binding site that was identified in all three structures. Comparisons suggest that this may represent a conserved structural feature of FabF relevant to fold stability. The new structures provide templates for structure-based ligand design and, together with the protocols and reagents, may underpin a target-based drug-discovery project for urgently needed antibacterials.
Structures of Pseudomonas aeruginosa beta-ketoacyl-(acyl-carrier-protein) synthase II (FabF) and a C164Q mutant provide templates for antibacterial drug discovery and identify a buried potassium ion and a ligand-binding site that is an artefact of the crystal form.,Baum B, Lecker LS, Zoltner M, Jaenicke E, Schnell R, Hunter WN, Brenk R Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):1020-6. doi:, 10.1107/S2053230X15010614. Epub 2015 Jul 28. PMID:26249693[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Baum B, Lecker LS, Zoltner M, Jaenicke E, Schnell R, Hunter WN, Brenk R. Structures of Pseudomonas aeruginosa beta-ketoacyl-(acyl-carrier-protein) synthase II (FabF) and a C164Q mutant provide templates for antibacterial drug discovery and identify a buried potassium ion and a ligand-binding site that is an artefact of the crystal form. Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):1020-6. doi:, 10.1107/S2053230X15010614. Epub 2015 Jul 28. PMID:26249693 doi:http://dx.doi.org/10.1107/S2053230X15010614
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