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

作者:Sun Tianjun; Hayakawa Koto; Fraser Marie E*
来源:Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 2011, 67: 1168-1172.
DOI:10.1107/S1744309111028363

摘要

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 angstrom resolution. The structure shows ADP-Mg2+ 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.

  • 出版日期2011-10

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