Ontology highlight
ABSTRACT:
SUBMITTER: Wei X
PROVIDER: S-EPMC10115795 | biostudies-literature | 2023 Apr
REPOSITORIES: biostudies-literature
Wei Xuepeng X Schultz Kollin K Pepper Hannah L HL Megill Emily E Vogt Austin A Snyder Nathaniel W NW Marmorstein Ronen R
Nature communications 20230419 1
ATP citrate lyase (ACLY) is the predominant nucleocytosolic source of acetyl-CoA and is aberrantly regulated in many diseases making it an attractive therapeutic target. Structural studies of ACLY reveal a central homotetrameric core citrate synthase homology (CSH) module flanked by acyl-CoA synthetase homology (ASH) domains, with ATP and citrate binding the ASH domain and CoA binding the ASH-CSH interface to produce acetyl-CoA and oxaloacetate products. The specific catalytic role of the CSH mo ...[more]