F
IPR005726

ATP synthase alpha chain, archaea

InterPro entry
Short nameATP_synth_asu_arc
Overlapping
homologous
superfamilies
 
family relationships

Description

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.

A-ATPases (or A1A0-ATPase) (
3.6.3.14
) are found exclusively in Archaea and display a close resemblance in structure and subunit composition with V-ATPases, although their function in both ATP synthesis and ATP hydrolysis is closer to that of F-ATPases
[1]
. A-ATPases are composed of two linked complexes: the A1 complex consisting of seven subunits contains the catalytic core that synthesizes/hydrolyses ATP, while the A0 complex consisting of at least two subunits forms the membrane-spanning pore
[3]
. The rotary motor in A-ATPases is composed of only two subunits, the stator subunit I and the rotor subunit C
[2]
. A-ATPases may have arisen as an adaptation to the different cellular needs and the more extreme environmental conditions faced by Archaeal species.

This entry represents the alpha subunit from the A1 complex of A-ATPases. The A1 complex contains three copies each of subunits alpha (or A) and beta (or B) (
IPR005724
), both of which form the headpiece that participates in nucleotide binding. However, only the alpha subunit is catalytic, the beta subunit being regulatory in function
[4]
.

References

1.Structure and function of the A1A0-ATPases from methanogenic Archaea. Muller V, Ruppert C, Lemker T. J. Bioenerg. Biomembr. 31, 15-27, (1999). View articlePMID: 10340845

2.An exceptional variability in the motor of archael A1A0 ATPases: from multimeric to monomeric rotors comprising 6-13 ion binding sites. Muller V. J. Bioenerg. Biomembr. 36, 115-25, (2004). View articlePMID: 15168615

3.Subunit structure and organization of the genes of the A1A0 ATPase from the Archaeon Methanosarcina mazei Go1. Wilms R, Freiberg C, Wegerle E, Meier I, Mayer F, Muller V. J. Biol. Chem. 271, 18843-52, (1996). View articlePMID: 8702544

4.Three-dimensional organization of the archaeal A1-ATPase from Methanosarcina mazei Go1. Coskun U, Radermacher M, Muller V, Ruiz T, Gruber G. J. Biol. Chem. 279, 22759-64, (2004). View articlePMID: 14988401

Further reading

5. F-type or V-type? The chimeric nature of the archaebacterial ATP synthase. Schafer G, Meyering-Vos M. Biochim. Biophys. Acta 1101, 232-5, (1992). PMID: 1385979

6. F-and V-ATPases in the genus Thermus and related species. Radax C, Sigurdsson O, Hreggvidsson GO, Aichinger N, Gruber C, Kristjansson JK, Stan-Lotter H. Syst. Appl. Microbiol. 21, 12-22, (1998). PMID: 9741106

7. Regulation and isoform function of the V-ATPases. Toei M, Saum R, Forgac M. Biochemistry 49, 4715-23, (2010). View articlePMID: 20450191

8. New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0). Gruber G, Marshansky V. Bioessays 30, 1096-109, (2008). View articlePMID: 18937357

9. Mechanisms of ATPases--a multi-disciplinary approach. Rappas M, Niwa H, Zhang X. Curr. Protein Pept. Sci. 5, 89-105, (2004). View articlePMID: 15078220

10. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. Cross RL, Muller V. FEBS Lett. 576, 1-4, (2004). View articlePMID: 15473999

GO terms

Cross References

Contributing Member Database Entry
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.