2F7K

Crystal Structure of Human Pyridoxal Kinase

2F7K の概要

• エントリーDOI: 10.2210/pdb2f7k/pdb
• 分子名称: Pyridoxal kinase (2 entities in total)
• 機能のキーワード: alpha-beta structure, transferase
• 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: 74134.59

構造登録者

Jiang, T.,Cao, P.,Gong, Y.,Tang, L. (登録日: 2005-12-01, 公開日: 2006-06-13, 最終更新日: 2024-03-13)

主引用文献

Cao, P.,Gong, Y.,Tang, L.,Leung, Y.C.,Jiang, T.
Crystal structure of human pyridoxal kinase
J.Struct.Biol., 154:327-332, 2006

PubMed Abstract: Pyridoxal kinase, a member of the ribokinase superfamily, catalyzes the ATP-dependent phosphorylation reaction of vitamin B6 and is an essential enzyme in the formation of pyridoxal-5'-phosphate, a key cofactor for over 100 enzymes. Pyridoxal kinase is thus regarded as a potential target for pharmacological agents. In this paper, we report the 2.8 angstroms crystal structure of human pyridoxal kinase (HPLK) expressed in Escherichia coli. The diffraction data revealed unexpected merohedral perfect twinning along the crystallographic c axis. Taking perfect twinning into account, the structure in dimeric form was well refined according to the CNS program. Structure comparison reveals that the key 12-residue peptide over the active site in HPLK is a beta-strand/loop/beta-strand flap, while the corresponding peptide in sheep brain enzyme adopts a loop conformation. Moreover, HPLK possesses a more hydrophobic ATP-binding pocket. This structure will facilitate further biochemical studies and structure-based design of drugs related to pyridoxal kinase.

PubMed: 16600635
DOI: 10.1016/j.jsb.2006.02.008

実験手法

X-RAY DIFFRACTION (2.8 Å)