SSF81660

Metal cation-transporting ATPase, ATP-binding domain N

SUPERFAMILY entry
Member databaseSUPERFAMILY
SUPERFAMILY typehomologous superfamily

Description
Imported from IPR023299

This superfamily represents the cytoplasmic domain N found in P-type ATPases. The cytoplasmic loops of the P-type ATPases form three separate modules, commonly named the A, P and N-domains
[2, 5]
. The N-domain comprises the nucleotide binding site
[1]
. This domain forms a seven-stranded antiparallel β-sheet with two additional β-strands forming a hairpin and five α-helices
[4]
.

P-ATPases (also known as E1-E2 ATPases) (
3.6.3.-
) are found in bacteria and in a number of eukaryotic plasma membranes and organelles
[3]
. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases, which transport specific types of ion: H+, Na+, K+, Mg2+, Ca2+, Ag+and Ag2+, Zn2+, Co2+, Pb2+, Ni2+, Cd2+, Cu+and Cu2+. P-ATPases can be composed of one or two polypeptides, and can usually assume two main conformations called E1 and E2.

References
Imported from IPR023299

1.Inter-domain motions of the N-domain of the KdpFABC complex, a P-type ATPase, are not driven by ATP-induced conformational changes. Haupt M, Bramkamp M, Coles M, Altendorf K, Kessler H. J. Mol. Biol. 342, 1547-58, (2004). View articlePMID: 15364580

2.Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Toyoshima C, Nomura H, Tsuda T. Nature 432, 361-8, (2004). View articlePMID: 15448704

3.Evolution of substrate specificities in the P-type ATPase superfamily. Axelsen KB, Palmgren MG. J. Mol. Evol. 46, 84-101, (1998). View articlePMID: 9419228

4.The crystallographic structure of Na,K-ATPase N-domain at 2.6A resolution. Hakansson KO. J. Mol. Biol. 332, 1175-82, (2003). View articlePMID: 14499619

5.Improved Model of Proton Pump Crystal Structure Obtained by Interactive Molecular Dynamics Flexible Fitting Expands the Mechanistic Model for Proton Translocation in P-Type ATPases. Focht D, Croll TI, Pedersen BP, Nissen P. Front Physiol 8, 202, (2017). PMID: 28443028

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