3PFF

Truncated human atp-citrate lyase with ADP and tartrate bound

Summary for 3PFF

• Entry DOI: 10.2210/pdb3pff/pdb
• Related: 3MWD 3MWE
• Descriptor: ATP-citrate synthase, MAGNESIUM ION, L(+)-TARTARIC ACID, ... (5 entities in total)
• Functional Keywords: phosphohistidine, organic acid, atp-grasp, lyase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P53396
• Total number of polymer chains: 1
• Total formula weight: 91437.71

Authors

Fraser, M.E.,Sun, T. (deposition date: 2010-10-28, release date: 2011-10-12, Last modification date: 2024-11-06)

Primary citation

Sun, T.,Hayakawa, K.,Fraser, M.E.
ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase.
Acta Crystallogr.,Sect.F, 67:1168-1172, 2011

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 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.

PubMed: 22102020
DOI: 10.1107/S1744309111028363

Experimental method

X-RAY DIFFRACTION (2.3 Å)