4y0a | pdb_00004y0a

Shikimate kinase from Acinetobacter baumannii in complex with shikimate

spinqualitylabelsall models 4y0a, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4y0a is a 1 chain structure with sequence from Acinetobacter baumannii AB307-0294. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.911Å Ligands: SKM, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M3KL09_ACIB3 Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.[HAMAP-Rule:MF_00109] Publication Abstract from PubMed Acinetobacter baumannii is an opportunistic Gram-negative pathogen that is an important cause of healthcare-associated infections exhibiting high mortality rates. Clinical isolates of multidrug-resistant (MDR) and extremely drug-resistant (XDR) A. baumannii strains are increasingly being observed. Compounding this concern is the dearth of new antibacterial agents in late-stage development that are effective against MDR and XDR A. baumannii. As part of an effort to address these concerns, two genes (aroA and aroC) of the shikimate pathway have previously been determined to be essential for the growth and survival of A. baumannii during host infection (i.e. to be essential in vivo). This study expands upon these results by demonstrating that the A. baumannii aroK gene, encoding shikimate kinase (SK), is also essential in vivo in a rat soft-tissue infection model. The crystal structure of A. baumannii SK in complex with the substrate shikimate and a sulfate ion that mimics the binding interactions expected for the beta-phosphate of ATP was then determined to 1.91 A resolution and the enzyme kinetics were characterized. The flexible shikimate-binding domain and LID region are compared with the analogous regions in other SK crystal structures. The impact of structural differences and sequence divergence between SKs from pathogenic bacteria that may influence antibiotic-development efforts is discussed. Structure of shikimate kinase, an in vivo essential metabolic enzyme in the nosocomial pathogen Acinetobacter baumannii, in complex with shikimate.,Sutton KA, Breen J, MacDonald U, Beanan JM, Olson R, Russo TA, Schultz LW, Umland TC Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1736-44. doi:, 10.1107/S139900471501189X. Epub 2015 Jul 31. PMID:26249354 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Shikimate kinase 3D structures

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