D
IPR011761

ATP-grasp fold

InterPro entry
Short nameATP-grasp
domain relationships

Description

The ATP-grasp superfamily currently includes 17 groups of enzymes, catalysing 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 characterised by two α-β subdomains that grasp the ATP molecule between them. Each subdomain provides a variable loop that forms part of the active site, with regions from other domains also contributing to the active site, even though these other domains are not conserved between the various ATP-grasp enzymes
[4]
.

References

1.A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Galperin MY, Koonin EV. Protein Sci. 6, 2639-43, (1997). View articlePMID: 9416615

2.Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution. Fan C, Moews PC, Walsh CT, Knox JR. Science 266, 439-43, (1994). View articlePMID: 7939684

3.Structural classification of proteins: new superfamilies. Murzin AG. Curr. Opin. Struct. Biol. 6, 386-94, (1996). View articlePMID: 8804825

4.A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli. Fan C, Moews PC, Shi Y, Walsh CT, Knox JR. Proc. Natl. Acad. Sci. U.S.A. 92, 1172-6, (1995). View articlePMID: 7862655

GO terms

biological process

  • None

cellular component

  • None

Cross References

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