4nb4

Pantothenamide-bound Pantothenate kinase from Staphylococcus aureus

spinqualitylabelsall models 4nb4, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nb4 is a 8 chain structure with sequence from Staphylococcus aureus subsp. aureus MRSA252. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: ADP, MG, SH3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COAW_STAAS Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Publication Abstract from PubMed Pantothenate kinase (PanK) is the rate-limiting enzyme in Coenzyme A biosynthesis, catalyzing the ATP-dependent phosphorylation of pantothenate. We solved the co-crystal structures of PanKs from Staphylococcus aureus (SaPanK) and Klebsiella pneumonia (KpPanK) with N-[2-(1,3-benzodioxol-5-yl)ethyl] pantothenamide (N354-Pan). Two different N354-Pan conformers interact with polar/nonpolar mixed residues in SaPanK and aromatic residues in KpPanK. Additionally, phosphorylated N354-Pan is found at the closed active site of SaPanK but not at the open active site of KpPanK, suggesting an exchange of the phosphorylated product with a new N354-Pan only in KpPanK. Together, pantothenamides conformational flexibility and binding pocket are two key considerations for selective compound design. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. Structural characterization of a new N-substituted pantothenamide bound to pantothenate kinases from Klebsiella pneumonia and Staphylococcus aureus.,Hughes SJ, Antoshchenko T, Kim KP, Smil D, Park HW Proteins. 2014 Jan 28. doi: 10.1002/prot.24524. PMID:24470271 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pantothenate kinase 3D structures

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