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


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.

SUBMITTER: Sun T 

PROVIDER: S-EPMC3212355 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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

Sun Tianjun T   Hayakawa Koto K   Fraser Marie E ME  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110924 Pt 10


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  ...[more]

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