![]() |
|
PROSITE documentation PDOC50975 |
The ATP-grasp superfamily currently includes 17 groups of enzymes, catalyzing ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule [1]. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate. For example, DD-ligase transfers phosphate from ATP to D-alanine on the first step of catalysis. On the second step the resulting acylphosphate is attacked by a second D-alanine to produce a DD dipeptide following phosphate elimination [2].
The ATP-grasp domain contains three conserved motifs, corresponding to the phosphate binding loop and the Mg(2+) binding site [3]. The fold is characterized by two α-β subdomains that grasp the ATP molecule between them (see <PDB:1IOW>). Each subdomain provides a variable loop that forms a part of the active site, completed by region of other domains not conserved between the various ATP-grasp enzymes[4].
Proteins known to contain an ATP-grasp domain are listed below:
The profile we developed covers the entire ATP-grasp domain.
Last update:April 2004 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Galperin M.Y. Koonin E.V. |
Title | A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. | |
Source | Protein Sci. 6:2639-2643(1997). | |
PubMed ID | 9416615 |
2 | Authors | Fan C. Moews P.C. Walsh C.T. Knox J.R. |
Title | Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution. | |
Source | Science 266:439-443(1994). | |
PubMed ID | 7939684 |
3 | Authors | Murzin A.G. |
Title | Structural classification of proteins: new superfamilies. | |
Source | Curr. Opin. Struct. Biol. 6:386-394(1996). | |
PubMed ID | 8804825 |
4 | Authors | Fan C. Moews P.C. Shi Y. Walsh C.T. Knox J.R. |
Title | A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli. | |
Source | Proc. Natl. Acad. Sci. U.S.A. 92:1172-1176(1995). | |
PubMed ID | 7862655 |