7pps
From Proteopedia
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==apo FabB from Pseudomonas aeruginosa with single point mutation C161A== | ==apo FabB from Pseudomonas aeruginosa with single point mutation C161A== | ||
| - | <StructureSection load='7pps' size='340' side='right'caption='[[7pps]]' scene=''> | + | <StructureSection load='7pps' size='340' side='right'caption='[[7pps]], [[Resolution|resolution]] 1.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PPS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7pps]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_UCBPP-PA14 Pseudomonas aeruginosa UCBPP-PA14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PPS FirstGlance]. <br> |
| - | </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=7pps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pps OCA], [https://pdbe.org/7pps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pps RCSB], [https://www.ebi.ac.uk/pdbsum/7pps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pps ProSAT]</span></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]] 1.3Å</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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=7pps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pps OCA], [https://pdbe.org/7pps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pps RCSB], [https://www.ebi.ac.uk/pdbsum/7pps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pps ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FABB_PSEAB FABB_PSEAB] Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can also use unsaturated fatty acids. Catalyzes a key reaction in unsaturated fatty acid (UFA) synthesis, the elongation of the cis-3-decenoyl-ACP produced by FabA.[UniProtKB:P0A953] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Background: FabB (3-oxoacyl-[acyl-carrier-protein] synthase 1) is part of the fatty acid synthesis II pathway found in bacteria and a potential target for antibiotics. The enzyme catalyses the Claisen condensation of malonyl-ACP (acyl carrier protein) with acyl-ACP via an acyl-enzyme intermediate. Here, we report the crystal structure of the intermediate-mimicking Pseudomonas aeruginosa FabB ( PaFabB) C161A variant. Methods: His-tagged PaFabB C161A was expressed in E. coli Rosetta DE3 pLysS cells, cleaved by TEV protease and purified using affinity and size exclusion chromatography. Commercial screens were used to identify suitable crystallization conditions which were subsequently improved to obtain well diffracting crystals. Results: We developed a robust and efficient system for recombinant expression of PaFabB C161A. Conditions to obtain well diffracting crystals were established. The crystal structure of PaFabB C161A was solved by molecular replacement at 1.3 A resolution. Binding site comparison between PaFabB and PaFabF revealed a conserved malonyl binding site but differences in the fatty acid binding channel. Conclusions: The PaFabB C161A crystal structure can be used as a template to facilitate the design of FabB inhibitors. | ||
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| + | Crystal structure of Pseudomonas aeruginosa FabB C161A, a template for structure-based design for new antibiotics.,Yadrykhins'ky V, Georgiou C, Brenk R F1000Res. 2021 Nov 1;10. doi: 10.12688/f1000research.74018.2. eCollection 2021. PMID:35136566<ref>PMID:35136566</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7pps" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa UCBPP-PA14]] | ||
[[Category: Brenk R]] | [[Category: Brenk R]] | ||
[[Category: Georgiou C]] | [[Category: Georgiou C]] | ||
[[Category: Yadrykhinsky V]] | [[Category: Yadrykhinsky V]] | ||
Current revision
apo FabB from Pseudomonas aeruginosa with single point mutation C161A
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