5cg1 | pdb_00005cg1

Crystal structure of E. coli FabI bound to the carbamoylated benzodiazaborine inhibitor 14b.

spinqualitylabelsall models 5cg1, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cg1 is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.07Å Ligands: BBN, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FABI_ECOLI Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis. Publication Abstract from PubMed Enoyl-ACP reductase, the last enzyme of the fatty-acid biosynthetic pathway, is the molecular target for several successful antibiotics such as the tuberculosis therapeutic isoniazid. It is currently under investigation as a narrow-spectrum antibiotic target for the treatment of several types of bacterial infections. The diazaborine family is a group of boron heterocycle-based synthetic antibacterial inhibitors known to target enoyl-ACP reductase. Development of this class of molecules has thus far focused solely on the sulfonyl-containing versions. Here, the requirement for the sulfonyl group in the diazaborine scaffold was investigated by examining several recently characterized enoyl-ACP reductase inhibitors that lack the sulfonyl group and exhibit additional variability in substitutions, size and flexibility. Biochemical studies are reported showing the inhibition of Escherichia coli enoyl-ACP reductase by four diazaborines, and the crystal structures of two of the inhibitors bound to E. coli enoyl-ACP reductase solved to 2.07 and 2.11 A resolution are reported. The results show that the sulfonyl group can be replaced with an amide or thioamide without disruption of the mode of inhibition of the molecule. Crystallographic insights into the structure-activity relationships of diazaborine enoyl-ACP reductase inhibitors.,Jordan CA, Sandoval BA, Serobyan MV, Gilling DH, Groziak MP, Xu HH, Vey JL Acta Crystallogr F Struct Biol Commun. 2015 Dec 1;71(Pt 12):1521-30. doi:, 10.1107/S2053230X15022098. Epub 2015 Nov 27. PMID:26625295 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enoyl-Acyl-Carrier Protein Reductase 3D structures

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