3FHY

Crystal structure of D235N mutant of human pyridoxal kinase

3FHY の概要

• エントリーDOI: 10.2210/pdb3fhy/pdb
• 関連するPDBエントリー: 3FHX
• 分子名称: Pyridoxal kinase, MAGNESIUM ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: beta sheet with alpha helix, atp complex, metal ion, transferase, acetylation, alternative splicing, atp-binding, cytoplasm, kinase, metal-binding, nucleotide-binding, zinc
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: O00764
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73491.65

構造登録者

Safo, M.K.,Gandhi, A.K.,Musayev, F.N.,Ghatge, M.,Di Salvo, M.L.,Schirch, V. (登録日: 2008-12-10, 公開日: 2008-12-23, 最終更新日: 2023-09-06)

主引用文献

Gandhi, A.K.,Ghatge, M.S.,Musayev, F.N.,Sease, A.,Aboagye, S.O.,di Salvo, M.L.,Schirch, V.,Safo, M.K.
Kinetic and structural studies of the role of the active site residue Asp235 of human pyridoxal kinase.
Biochem.Biophys.Res.Commun., 381:12-15, 2009

PubMed Abstract: 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.

PubMed: 19351586
DOI: 10.1016/j.bbrc.2009.01.170

実験手法

X-RAY DIFFRACTION (2.3 Å)