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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
polycyclic hydrocarbon
protein binding
amino acid sequence
antagonists and inhibitors
enzyme active site
enzyme specificity
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
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.
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structures of the Y. pestis ?-ketoacyl-acyl carrier protein synthases FabF and FabH, and compared these with the unpublished, deposited structure of Y. pestis FabB.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
ISSN: 2045-2322
DOI: 10.1038/srep14797
Rights: Attribution 4.0 International
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