2f7k
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Crystal Structure of Human Pyridoxal Kinase
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Paroxysmal nonkinesigenic dyskinesia OMIM:[609023], Polycystic kidney and hepatic disease OMIM:[606702]
About this StructureAbout this Structure
2F7K is a Single protein structure of sequence from Homo sapiens. Active as Pyridoxal kinase, with EC number 2.7.1.35 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human pyridoxal kinase., Cao P, Gong Y, Tang L, Leung YC, Jiang T, J Struct Biol. 2006 Jun;154(3):327-32. Epub 2006 Mar 20. PMID:16600635
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