|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 . 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 .
The ATP-grasp domain contains three conserved motifs, corresponding to the phosphate binding loop and the Mg(2+) binding site . 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.
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).|
|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.|
|Title||Structural classification of proteins: new superfamilies.|
|Source||Curr. Opin. Struct. Biol. 6:386-394(1996).|
|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).|