D
IPR013650

ATP-grasp fold, succinyl-CoA synthetase-type

InterPro entry
Short nameATP-grasp_succ-CoA_synth-type
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 a part of the active site, completed by region of other domains not conserved between the various ATP-grasp enzymes
[4]
.

The ATP-grasp domain represented by this entry is found primarily in succinyl-CoA synthetases (
6.2.1.5
).

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

Cross References

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