ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1168-72. doi: 10.1107/S1744309111028363. Epub 2011 Sep 24.

Abstract

Human ATP-citrate lyase (EC 2.3.3.8) is the cytoplasmic enzyme that catalyzes the production of acetyl-CoA from citrate, CoA and ATP. The amino-terminal portion of the enzyme, containing residues 1-817, was crystallized in the presence of tartrate, ATP and magnesium ions. The crystals diffracted to 2.3 Å resolution. The structure shows ADP-Mg(2+) bound to the domain that possesses the ATP-grasp fold. The structure demonstrates that this crystal form could be used to investigate the structures of complexes with inhibitors of ATP-citrate lyase that bind at either the citrate- or ATP-binding site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP Citrate (pro-S)-Lyase / chemistry*
  • ATP Citrate (pro-S)-Lyase / metabolism
  • Adenosine Diphosphate / chemistry*
  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / chemistry*
  • Adenosine Triphosphate / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • Escherichia coli / enzymology
  • Humans
  • Magnesium / chemistry*
  • Magnesium / metabolism
  • Models, Molecular
  • Protein Interaction Domains and Motifs*
  • Structural Homology, Protein

Substances

  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • ATP Citrate (pro-S)-Lyase
  • Magnesium

Associated data

  • PDB/3PFF