1NW1

Crystal Structure of Choline Kinase

Summary for 1NW1

• Entry DOI: 10.2210/pdb1nw1/pdb
• Descriptor: Choline kinase (49.2 kD), CALCIUM ION (3 entities in total)
• Functional Keywords: choline kinase, phospholipid synthesis, protein kinase fold, transferase
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 98682.13

Authors

Peisach, D.,Gee, P.,Kent, C.,Xu, Z. (deposition date: 2003-02-05, release date: 2003-06-10, Last modification date: 2024-02-14)

Primary citation

Peisach, D.,Gee, P.,Kent, C.,Xu, Z.
The Crystal Structure of Choline Kinase Reveals a Eukaryotic Protein Kinase Fold
Structure, 11:703-713, 2003

PubMed Abstract: 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.

PubMed: 12791258
DOI: 10.1016/S0969-2126(03)00094-7

Experimental method

X-RAY DIFFRACTION (2.02 Å)