3fhy | pdb_00003fhy

Crystal structure of D235N mutant of human pyridoxal kinase

spinqualitylabelsall models 3fhy, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fhy is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, MG, MPD, NA, SO4 Related: 3fhx Gene: C21orf124, C21orf97, PDXK, PKH, PNK (HUMAN) Activity: Pyridoxal kinase, with EC number 2.7.1.35 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PDXK_HUMAN] Required for synthesis of pyridoxal-5-phosphate from vitamin B6. Publication Abstract from PubMed Pyridoxal kinase catalyzes the phosphorylation of pyridoxal (PL) to pyridoxal 5'-phosphate (PLP). A D235A variant shows 7-fold and 15-fold decreases in substrate affinity and activity, respectively. A D235N variant shows approximately 2-fold decrease in both PL affinity and activity. The crystal structure of D235A (2.5 A) shows bound ATP, PL and PLP, while D235N (2.3 A) shows bound ATP and sulfate. These results document the role of Asp235 in PL kinase activity. The observation that the active site of PL kinase can accommodate both ATP and PLP suggests that formation of a ternary Enz.PLP.ATP complex could occur in the wild-type enzyme, consistent with severe MgATP substrate inhibition of PL kinase in the presence of PLP. Kinetic and structural studies of the role of the active site residue Asp235 of human pyridoxal kinase.,Gandhi AK, Ghatge MS, Musayev FN, Sease A, Aboagye SO, di Salvo ML, Schirch V, Safo MK Biochem Biophys Res Commun. 2009 Mar 27;381(1):12-5. Epub 2009 Feb 4. PMID:19351586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyridoxal kinase

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