4ne2 | pdb_00004ne2

Pantothenamide-bound Pantothenate Kinase from Klebsiella pneumoniae

spinqualitylabelsall models 4ne2, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ne2 is a 2 chain structure with sequence from Klep3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG, SH2 Related: 4nb4 Gene: coaA, KPK_5321, UUU_44690 (KLEP3) Activity: Pantothenate kinase, with EC number 2.7.1.33 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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

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