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Protein structural motif From Wikipedia, the free encyclopedia
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.[2][3]
| ATP-grasp domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Cartoon representation of the X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli. , which belongs to the ATP grasp superfamily (PDB: 1gso).[1] | |||||||||
| Identifiers | |||||||||
| Symbol | ATP-grasp | ||||||||
| Pfam | PF02222 | ||||||||
| Pfam clan | CL0179 | ||||||||
| ECOD | 206.1.3 | ||||||||
| InterPro | IPR013815 | ||||||||
| |||||||||
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]
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]
The ATP-grasp fold is evolutionarily conserved across different enzyme families and its presence is ubiquitous across prokaryotes and eukaryotes.[3]
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]
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