ATPase

ATPase is an enzyme which catalyzes the breakdown of ATP into ADP and a phosphate ion. This dephosphorylation releases energy which the enzyme uses to drive other reactions^[1]. The F1/0 ATPase is called ATP synthase synthesises the reverse reaction, i.e., the addition of phosphate to ADP to form ATP^[2]. ATPase types include:

F-ATPase - the prime producers of ATP^[3]. For details see Alice Clark/ATPsynthase;
V-ATPase or Vacuolar-type H+ ATPase couples the energy to proton transport across membranes. For details see V-ATPase;
A-ATPase are found in archaea. For details see A-ATP Synthase;
P-ATPase transport ions^[4]
E-ATPase hydrolyze extracellular ATP^[5].
MipZ is an ATPase which forms a complex with the chromosome partitioning protein ParB and is responsible for the regulation of FtsZ ring formation.

ATPase domains include metal-binding domain (MBD) and nucleotide-binding domain (NBD). For more details see:

Cu transporting ATPase are in P(1B)-Type Cu(I) Transporting ATPases ATP7A and ATP7B.
Na/K transporting ATPase are in Sodium-Potassium ATPase.
H/K transporting ATPase are in Esomeprazole and H+/K+ - ATPase Interaction.
Transitional endoplasmic reticulum ATPase are in Valosin Containing Protein D120.
Central stalk in F(1)-ATPase is described in A-ATP Synthase
RuvBL1/RuvBL2 complex (ATPase)
For Ter-ATPase see Valosin Containing Protein D120

An ATPase, Human RuvB-like 1 dodecamer complex with ADP (PDB code 2c9o)

Drag the structure with the mouse to rotate

3D Printed Physical Model of ATP Synthase3D Printed Physical Model of ATP Synthase

Shown below is a 3D printed physical model of the Respiration Electron Transport Chain. Complex I is colored red, complex II is purple, complex III is green, complex IV is blue and the atp synthase protein is colored orange, yellow and red.

The MSOE Center for BioMolecular ModelingThe MSOE Center for BioMolecular Modeling

The MSOE Center for BioMolecular Modeling uses 3D printing technology to create physical models of protein and molecular structures, making the invisible molecular world more tangible and comprehensible. To view more protein structure models, visit our Model Gallery.

3D Structures of ATPase3D Structures of ATPase

ATPase 3D structures

ReferencesReferences

↑ Rappas M, Niwa H, Zhang X. Mechanisms of ATPases--a multi-disciplinary approach. Curr Protein Pept Sci. 2004 Apr;5(2):89-105. doi: 10.2174/1389203043486874. PMID:15078220 doi:http://dx.doi.org/10.2174/1389203043486874
↑ Neupane P, Bhuju S, Thapa N, Bhattarai HK. ATP Synthase: Structure, Function and Inhibition. Biomol Concepts. 2019 Mar 7;10(1):1-10. doi: 10.1515/bmc-2019-0001. PMID:30888962 doi:http://dx.doi.org/10.1515/bmc-2019-0001
↑ Abrahams JP, Leslie AG, Lutter R, Walker JE. Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature. 1994 Aug 25;370(6491):621-8. PMID:8065448 doi:http://dx.doi.org/10.1038/370621a0
↑ Chan H, Babayan V, Blyumin E, Gandhi C, Hak K, Harake D, Kumar K, Lee P, Li TT, Liu HY, Lo TC, Meyer CJ, Stanford S, Zamora KS, Saier MH Jr. The p-type ATPase superfamily. J Mol Microbiol Biotechnol. 2010;19(1-2):5-104. doi: 10.1159/000319588. Epub 2010, Oct 20. PMID:20962537 doi:http://dx.doi.org/10.1159/000319588
↑ Plesner L. Ecto-ATPases: identities and functions. Int Rev Cytol. 1995;158:141-214. doi: 10.1016/s0074-7696(08)62487-0. PMID:7721538 doi:http://dx.doi.org/10.1016/s0074-7696(08)62487-0

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Alexander Berchansky, Jaime Prilusky, Michal Harel, Wayne Decatur, Mark Hoelzer, Karsten Theis

[1] Rappas M, Niwa H, Zhang X. Mechanisms of ATPases--a multi-disciplinary approach. Curr Protein Pept Sci. 2004 Apr;5(2):89-105. doi: 10.2174/1389203043486874. PMID:15078220 doi:http://dx.doi.org/10.2174/1389203043486874

[2] Neupane P, Bhuju S, Thapa N, Bhattarai HK. ATP Synthase: Structure, Function and Inhibition. Biomol Concepts. 2019 Mar 7;10(1):1-10. doi: 10.1515/bmc-2019-0001. PMID:30888962 doi:http://dx.doi.org/10.1515/bmc-2019-0001

[3] Abrahams JP, Leslie AG, Lutter R, Walker JE. Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature. 1994 Aug 25;370(6491):621-8. PMID:8065448 doi:http://dx.doi.org/10.1038/370621a0

[4] Chan H, Babayan V, Blyumin E, Gandhi C, Hak K, Harake D, Kumar K, Lee P, Li TT, Liu HY, Lo TC, Meyer CJ, Stanford S, Zamora KS, Saier MH Jr. The p-type ATPase superfamily. J Mol Microbiol Biotechnol. 2010;19(1-2):5-104. doi: 10.1159/000319588. Epub 2010, Oct 20. PMID:20962537 doi:http://dx.doi.org/10.1159/000319588

[5] Plesner L. Ecto-ATPases: identities and functions. Int Rev Cytol. 1995;158:141-214. doi: 10.1016/s0074-7696(08)62487-0. PMID:7721538 doi:http://dx.doi.org/10.1016/s0074-7696(08)62487-0

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