Open AccessADP–Mg 2+ bound to the ATP‐grasp domain of ATP‐citrate lyase
Author(s) -
Sun Tianjun,
Hayakawa Koto,
Fraser Marie E.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111028363
Subject(s) - atp citrate lyase , lyase , citrate synthase , enzyme , adenosine triphosphate , tartrate , chemistry , transferase , biochemistry , stereochemistry , crystallography
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.