Article · Wikipedia archive · Last revised Aug 10, 2026

ATP-grasp

In molecular biology, the ATP-grasp fold is a unique ATP-binding protein structural motif made of two α+β subdomains that "grasp" a molecule of ATP between them. ATP-grasp proteins have ATP-dependent carboxylate-amine/thiol ligase activity.

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ATP-grasp domain
Ribbon diagram of glycinamide ribonucleotide synthetase (1gso​) demonstrating the ATP grasp superfamily fold.1
Identifiers
SymbolATP-grasp
PfamPF02222
Pfam clanCL0179
ECOD206.1.3
InterProIPR013815
Available protein structures:
PDB  IPR013815 PF02222 (ECOD; PDBsum)  
AlphaFold

In molecular biology, the ATP-grasp fold is a unique ATP-binding protein structural motif made of two α+β subdomains that "grasp" a molecule of ATP between them. ATP-grasp proteins have ATP-dependent carboxylate-amine/thiol ligase activity.23

Structure

Proteins of the ATP-grasp family have an overall structural configuration organised into three domains referred to as the N-terminal domain (or A-domain), the central domain (or B-domain), and the C-terminal domain (or C-domain).3

Function

ATP-grasp enzymes catalyse the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol group-containing molecule. The reactions typically involve formation of acylphosphate intermediates. These enzymes are involved in various metabolic pathways including purine biosynthesis, fatty acid synthesis, and gluconeogenesis.4

Examples of proteins containing this domain

Evolution and distribution

The ATP-grasp fold is evolutionarily conserved across different enzyme families and its presence is ubiquitous across prokaryotes and eukaryotes.3

Use in research

Researchers have developed several types of inhibitors for these enzymes, including mechanism-based inhibitors, ATP-competitive inhibitors, and non-competitive inhibitors. Some ATP-grasp enzymes are being studied as potential targets for antibiotics and anti-obesity drugs.3

References

References

  1. Wang W, Kappock TJ, Stubbe J, Ealick SE (November 1998). "X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli". Biochemistry. 37 (45): 15647–15662. doi:10.1021/bi981405n. PMID 9843369.
  2. Eroglu B, Powers-Lee SG (November 2002). "Mutational analysis of ATP-grasp residues in the two ATP sites of Saccharomyces cerevisiae carbamoyl phosphate synthetase". Archives of Biochemistry and Biophysics. 407 (1): 1–9. doi:10.1016/s0003-9861(02)00510-6. PMID 12392708.
  3. Fawaz MV, Topper ME, Firestine SM (December 2011). "The ATP-grasp enzymes". Bioorganic Chemistry. 39 (5–6): 185–191. doi:10.1016/j.bioorg.2011.08.004. PMC 3243065. PMID 21920581.
  4. Galperin MY, Koonin EV (December 1997). "A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity". Protein Science. 6 (12): 2639–2643. doi:10.1002/pro.5560061218. PMC 2143612. PMID 9416615.
  5. https://pmc.ncbi.nlm.nih.gov/articles/PMC9353652/
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