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TitleAllosteric role of the citrate synthase homology domain of ATP citrate lyase.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2247, Year 2023
Publish dateApr 19, 2023
AuthorsXuepeng Wei / Kollin Schultz / Hannah L Pepper / Emily Megill / Austin Vogt / Nathaniel W Snyder / Ronen Marmorstein /
PubMed AbstractATP 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 ...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 module and an essential D1026A residue contained within it has been a matter of debate. Here, we report biochemical and structural analysis of an ACLY-D1026A mutant demonstrating that this mutant traps a (3S)-citryl-CoA intermediate in the ASH domain in a configuration that is incompatible with the formation of acetyl-CoA, is able to convert acetyl-CoA and OAA to (3S)-citryl-CoA in the ASH domain, and can load CoA and unload acetyl-CoA in the CSH module. Together, this data support an allosteric role for the CSH module in ACLY catalysis.
External linksNat Commun / PubMed:37076498 / PubMed Central
MethodsEM (single particle)
Resolution2.2 - 2.8 Å
Structure data

24479

7rig

EMDB-24479, PDB-7rig:
Structure of ACLY-D1026A-substrates
Method: EM (single particle) / Resolution: 2.2 Å

24511

7rkz

EMDB-24511, PDB-7rkz:
Structure of ACLY D1026A-substrates-asym-int
Method: EM (single particle) / Resolution: 2.6 Å

24577

7rmp

EMDB-24577, PDB-7rmp:
Structure of ACLY D1026A - substrates-asym
Method: EM (single particle) / Resolution: 2.7 Å

29668

8g1e

EMDB-29668, PDB-8g1e:
Structure of ACLY-D1026A-products-asym
Method: EM (single particle) / Resolution: 2.8 Å

29669

8g1f

EMDB-29669, PDB-8g1f:
Structure of ACLY-D1026A-products
Method: EM (single particle) / Resolution: 2.4 Å

29739

8g5c

EMDB-29739, PDB-8g5c:
Structure of ACLY-D1026A-substrates, local refinement of ASH domain
Method: EM (single particle) / Resolution: 2.2 Å

29740

8g5d

EMDB-29740, PDB-8g5d:
Structure of ACLY-D1026A-products, local refinement of ASH domain
Method: EM (single particle) / Resolution: 2.5 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-Q5B:
(3S)-citryl-Coenzyme A

ChemComp-FLC:
CITRATE ANION / Citric acid


ChemComp, No image

ChemComp-UNL:
Unknown ligand

ChemComp-COA:
COENZYME A / Coenzyme A

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-HOH:
WATER / Water

ChemComp-ACO:
ACETYL COENZYME *A / Acetyl-CoA

ChemComp-OAA:
OXALOACETATE ION / Oxaloacetic acid

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / mutant / LYASE

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