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

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Citation

Sun T, Hayakawa K, Fraser ME

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.

PubMed ID
22102020 [ View in PubMed
]
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 A 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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
ATP-citrate synthaseP53396Details