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Title: | Structural Characterisation of the Beta-Ketoacyl-Acyl Carrier Protein Synthases, FabF and FabH, of Yersinia pestis | Authors: | Nanson, J.D Himiari, Z Swarbrick, C.M.D Forwood, J.K |
Keywords: | 3 oxoacyl acyl carrier protein synthase aminophenol derivative antiinfective agent enzyme inhibitor platencin polycyclic hydrocarbon protein binding amino acid sequence antagonists and inhibitors chemistry enzyme active site enzyme specificity enzymology genetics isolation and purification molecular docking molecular genetics molecular model protein conformation sequence alignment structure activity relation Yersinia pestis 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase Amino Acid Sequence Aminophenols Anti-Infective Agents Catalytic Domain Enzyme Inhibitors Models, Molecular Molecular Docking Simulation Molecular Sequence Data Polycyclic Compounds Protein Binding Protein Conformation Sequence Alignment Structure-Activity Relationship Substrate Specificity Yersinia pestis |
Issue Date: | 2015 | Publisher: | Nature Publishing Group | Citation: | Nanson, J.D, Himiari, Z, Swarbrick, C.M.D, Forwood, J.K (2015). Structural Characterisation of the Beta-Ketoacyl-Acyl Carrier Protein Synthases, FabF and FabH, of Yersinia pestis. Scientific Reports 5 : 14797. ScholarBank@NUS Repository. https://doi.org/10.1038/srep14797 | Rights: | Attribution 4.0 International | Abstract: | Yersinia pestis, the causative agent of bubonic, pneumonic, and septicaemic plague, remains a major public health threat, with outbreaks of disease occurring in China, Madagascar, and Peru in the last five years. The existence of multidrug resistant Y. pestis and the potential of this bacterium as a bioterrorism agent illustrates the need for new antimicrobials. The ?-ketoacyl-acyl carrier protein synthases, FabB, FabF, and FabH, catalyse the elongation of fatty acids as part of the type II fatty acid biosynthesis (FASII) system, to synthesise components of lipoproteins, phospholipids, and lipopolysaccharides essential for bacterial growth and survival. As such, these enzymes are promising targets for the development of novel therapeutic agents. We have determined the crystal structures of the Y. pestis ?-ketoacyl-acyl carrier protein synthases FabF and FabH, and compared these with the unpublished, deposited structure of Y. pestis FabB. Comparison of FabB, FabF, and FabH provides insights into the substrate specificities of these enzymes, and investigation of possible interactions with known ?-ketoacyl-acyl carrier protein synthase inhibitors suggests FabB, FabF and FabH may be targeted simultaneously to prevent synthesis of the fatty acids necessary for growth and survival. | Source Title: | Scientific Reports | URI: | https://scholarbank.nus.edu.sg/handle/10635/180426 | ISSN: | 2045-2322 | DOI: | 10.1038/srep14797 | Rights: | Attribution 4.0 International |
Appears in Collections: | Elements Staff Publications |
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