| 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 | ||||||||
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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]
- ^ 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.
- ^ 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.
- ^ 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.