Crystal structure of human pyridoxal kinase

Peng Cao, Yong Gong, Lin Tang, Yun Chung Leung, Tao Jiang

Research output: Journal article publicationJournal articleAcademic researchpeer-review

22 Citations (Scopus)


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 Å 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 β-strand/loop/β-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.
Original languageEnglish
Pages (from-to)327-332
Number of pages6
JournalJournal of Structural Biology
Issue number3
Publication statusPublished - 1 Jun 2006


  • Crystal structure
  • Human pyridoxal kinase
  • Perfect twinning
  • Pyridoxal-5′-phosphate

ASJC Scopus subject areas

  • Structural Biology


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