1nw1
Crystal Structure of Choline Kinase
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OverviewOverview
Choline kinase catalyzes the ATP-dependent phosphorylation of choline, the first committed step in the CDP-choline pathway for the biosynthesis of phosphatidylcholine. The 2.0 A crystal structure of a choline kinase from C. elegans (CKA-2) reveals that the enzyme is a homodimeric protein with each monomer organized into a two-domain fold. The structure is remarkably similar to those of protein kinases and aminoglycoside phosphotransferases, despite no significant similarity in amino acid sequence. Comparisons to the structures of other kinases suggest that ATP binds to CKA-2 in a pocket formed by highly conserved and catalytically important residues. In addition, a choline binding site is proposed to be near the ATP binding pocket and formed by several structurally flexible loops.
About this StructureAbout this Structure
1NW1 is a Single protein structure of sequence from Caenorhabditis elegans with as ligand. Active as Choline kinase, with EC number 2.7.1.32 Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of choline kinase reveals a eukaryotic protein kinase fold., Peisach D, Gee P, Kent C, Xu Z, Structure. 2003 Jun;11(6):703-13. PMID:12791258
Page seeded by OCA on Thu Feb 21 14:10:40 2008