7pps | pdb_00007pps

apo FabB from Pseudomonas aeruginosa with single point mutation C161A

spinqualitylabelsall models 7pps, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7pps is a 2 chain structure with sequence from Pseudomonas aeruginosa UCBPP-PA14. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.3Å Ligands: CL, EDO, IOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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] 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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