Structural Studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1NW1, 2CKO, 2CKP, 2CKQ, 2I7Q, and 2IG7.
CKα-2 originating from C. elegans, is a dimeric enzyme with each monomer being composed of two domains.The active site is located between the two domains. (See figure below) Its overall structure is similar to members of the eukaryotic protein kinase family. Mammalian choline kinases exists in either dimeric or tetrameric forms in solution. Structural studies carried out on CKα-2, have implied that the conserved residues in the CK family of enzymes could possible play a vital role in substrate binding as well as in the stabilization of catalytically important residues.
An enlarged view of the residues involved in the dimer interface between the S-shaped loop of the yellow subunit and the loop following helix A and strand 4 of the cyan subunit. Only residues that are involved in direct salt bridges, hydrogen bonds, or van der Waals interactions are shown. Salt bridges and hydrogen bonds, dashed lines; labels of residues from the yellow subunit, red; labels of residues from the cyan subunit, blue.
Read more about this topic: Choline Kinase
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