Member database | SFLD |
SFLD type | family |
Short name | C1.7:_P-type_atpase_like |
Description
Experimentally characterized enzymes in the P-type ATPase subgroup harness the energy of ATP to pump charged substrates across biological membranes. Mg2+ is required as a cofactor. ATPases in this group transport various molecules including heavy metals, phospholipids, K+, Ca2+, H+, Mg2+, Na+/K+, and H+/K+. P-type ATPases are made up of multiple structural domains. Only the catalytic domain, responsible for the hydrolysis of ATP, is part of the haloacid dehalogenase (HAD) superfamily
[1, 2, 3].
References
1.Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Toyoshima C, Nakasako M, Nomura H, Ogawa H. Nature 405, 647-55, (2000). View articlePMID: 10864315
2.Evolution of substrate specificities in the P-type ATPase superfamily. Axelsen KB, Palmgren MG. J. Mol. Evol. 46, 84-101, (1998). View articlePMID: 9419228
3.The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Aravind L, Galperin MY, Koonin EV. Trends Biochem. Sci. 23, 127-9, (1998). View articlePMID: 9584613
External Links
Representative structure
3skx: Crystal structure of the ATP binding domain of Archaeoglobus fulgidus COPB