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New page: left|200px|thumb|NMR Structure of ATPase [[1mo8]] {{STRUCTURE_1mo8| PDB=1mo8 | SIZE=300| SCENE= |right|CAPTION=ATPase 1mo8 }} ATPase catalyzes the breakdown o...
 
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[[Image:1mo8.png|left|200px|thumb|NMR Structure of ATPase [[1mo8]]]]
<StructureSection load='RuvBL12_12mer.pdb' size='400' side='right' scene='Journal:JSB:1/Cv/2' caption='An ATPase, Human RuvB-like 1 dodecamer complex with ADP (PDB code [[2c9o]])'>
{{STRUCTURE_1mo8|  PDB=1mo8  | SIZE=300| SCENE= |right|CAPTION=ATPase [[1mo8]] }}


[[ATPase]] catalyzes the breakdown of ATP to ADP and phosphate.  This reaction releases energy which is used by the cell in processes like moving solutes through molecular pumps against a gradient.  NBD is the nucleotide binding domain. MBD is the metal binding domain. The images at the left and at the right correspond to one representative ATPase, ''i.e.'' the NMR structure of rat ATPase ([[1mo8]]).


{{TOC limit|limit=2}}
[[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<ref>PMID:15078220</ref>. The F1/0 ATPase is called '''ATP synthase''' synthesises the reverse reaction, i.e., the addition of phosphate to ADP to form ATP<ref>PMID:30888962</ref>.  ATPase types include:<br />
* '''F-ATPase''' - the prime producers of ATP<ref>PMID:8065448</ref>.  For details see [[Alice Clark/ATPsynthase]];<br /> <!--Should there be a F-ATPase page for this like thee is for V-ATPase below? If one is made, I'd like to see links to the animations/movies referenced at https://twitter.com/NathanRoberts17/status/943428752113094656 there.-->
* '''V-ATPase''' or Vacuolar-type H+ ATPase couples the energy to proton transport across membranes. 


== 3D Structures of ATPase ==
ATPase is inhibited by [[Bedaquiline]] which is used as TB drug<ref>PMID:28807917</ref>.


Cu transporting ATPase
For details see [[V-ATPase]];<br />
* '''A-ATPase''' are found in archaea.  For details see [[A-ATP Synthase]];<br />
* '''P-ATPase''' transport ions<ref>PMID:20962537</ref><br />
* '''E-ATPase''' hydrolyze extracellular ATP<ref>PMID:7721538</ref>.  <br />
*  '''MipZ''' is an ATPase which forms a complex with the chromosome partitioning protein ParB and is responsible for the regulation of FtsZ ring formation.<br />
ATPase domains include metal-binding domain (MBD) and nucleotide-binding domain (NBD). For more details see:<br />
* '''ATPase RavA''' participates in the pathway which response to ahminoglycosides under anaerobic conditions and cell membrane regulation<ref>PMID:36127320</ref>.  <br />
* '''ATPase InvC''' energizes the apparatus needed for the entry of ''Salmonella typhimurium'' into mammalian cells<ref>PMID:8045880</ref>.  <br />
* '''Peroxisomal ATPase''' Pex1/Pex6 is essential for peroxisome formation<ref>PMID:37741838</ref>.  <br />
* '''INO8o ATPase''' is a component of the chromatin remodelling complex<ref>PMID:19062292</ref>.  <br />
*'''Cu transporting ATPase''' are in [[P(1B)-Type Cu(I) Transporting ATPases ATP7A and ATP7B]].<br />
*'''Na/K transporting ATPase''' are in [[Sodium-Potassium ATPase]].<br />
*'''H/K transporting ATPase''' are in [[Esomeprazole and H+/K+ - ATPase Interaction]].<br />
*'''Transitional endoplasmic reticulum ATPase''' are in [[Valosin Containing Protein D120]].<br />
*'''Central stalk in F(1)-ATPase''' is described in [[A-ATP Synthase]]<br />
*[[Journal:JSB:1|RuvBL1/RuvBL2 complex (ATPase)]]<br />


2kmv, 2kmx, 2arf – hATPase NBD – human – NMR
2kij - hATPase MBD – NMR
1yjr, 1yjt, 1yju, 1yjv - hATPase  (mutant) 6th soluble domain – NMR
1y3j, 1y3k - hATPase  5th soluble domain – NMR
1s6o, 1s6u - hATPase  2nd soluble domain – NMR
1q8l - hATPase  2nd MBD  – NMR
1aw0, 2aw0 - hATPase  4th MBD  – NMR
1kvi, 1kvj - hATPase  1st MBD  – NMR
3dxs - AtATPase MBD– Arabidopsis thaliana
3voy - AfATPase – Archaeoglobus fulgidus – CryoEM
2k1r - hATPase MBD+ ATOX1 – NMR
2rop, 2g9o, 2ga7 - hATPase MBD – NMR
2rml - BsATPase N-terminal – Bacillus subtilis – NMR
2gcf - sATPase N-terminal - Synechocystis – NMR
2iye - ATPase catalytic fragment – Sulfolobus solfataricus
1fvq, 1fvs - hATPase – NMR


Na/K transporting ATPase


3a3y - SaATPase+K+ouabain – Squalus acanthias
</StructureSection>
3b8e - pATPase a+BeF3 - pig
2hc8 –AfATPase CopA A domain
2b8e - AfATPase CopA NBD
2xze - SaATPase
3kdp, 3b8e – pATPase  – pig
1mo8, 1mo7 - ATPase alpha-1 – rat
1q3i - pATPase NBD


Ca transporting ATPase


3fgo - rATPase+CPA+AMPPCP – rabbit
==3D Printed Physical Model of ATP Synthase==
3b9r, 1xp5 - rATPase+AlF4
1wpg - rATPase+MgF4
2zbe – rATPase+BeF3
2zbf - rATPase+BeF3+TG
2zbg - rATPase+AlF4+TG
2zbd - rATPase+AlF4+ADP+Ca
2dqs - rATPase+AMPPCP
2c88, 2c8k - rATPase+AMPPCP+TG
1vfp - rATPase+AMPPCP
2ear, 2c8l - rATPase+TG
1iwo - rATPase
2agv - rATPase+TG+BHQ
2eas - rATPase+CPA
2eat - rATPase+CPA+GT
2eau - rATPase+CPA+curcumin
3ba6 - rATPase phosphoenzyme intermediate
3fpb - rATPase+ATP+cyclopiazonic acid
3fps, 2oa0 - rATPase+ADP+cyclopiazonic acid
2o9j - rATPase+MgF4+cyclopiazonic acid
1kju - rATPase E2 state
2c9m - rATPase Ca2E1 state
1t5s - rATPase Ca2E1 state+AMPPCP
1t5t - rATPase Ca2E1 state+ADP+AlF4
1su4 - rATPase +2Ca2
2by4 - rATPase HNE2 state+thapsigargin derivative


Zn transporting ATPase
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.
[[Image:atpSynthase1_centerForBioMolecularModeling.jpg |550px]]


2ofg, 2ofh - sATPase N-terminal – NMR


K+ transporting ATPase
====The MSOE Center for BioMolecular Modeling====


2a00, 2a29 - EcATPase NBD of KdpB+AMPPNP– Escherichia coli – NMR
[[Image:CbmUniversityLogo.jpg | left | 150px]]
1svj, 1u7q - EcATPase NBD of KdpB – NMR


As transporting ATPase
The [http://cbm.msoe.edu 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 [http://cbm.msoe.edu/educationalmedia/modelgallery/ Model Gallery].


1ii0, 1f48 - EcATPase
== 3D Structures of ATPase ==
1ihu – EcATPase+Mg+ADP+AlF3
[[ATPase 3D structures]]
1ii9 - EcATPase+AMPPNP
 
H+ transporting ATPase
 
3b8c  - AtATPase C terminal truncated
1mhs - ATPase – Neurospora crassa
 
Na+ transporting ATPase
 
2db4 - ATPase subunit K – Enterococcus hirae
1yce - ATPase rotor ring – Ilyobacter tartaricus
 
H/K transporting ATPase
 
1iwc, 1iwf - pATPase NBD
3ixz - pATPase a+AlF4
 
Mg transporting ATPase
 
3gwi – EcATPase P-1 NBD
 
Arg/ornithine transporting ATPase


3md0 – MtATPase+GDP – Mycobacterium tuberculosis
==References==
<references/>


1kmh - ATPase alpha subunit+tentoxin – spinach
[[Category:Topic Page]]
1h8e – cATPase+ADP+AlF4+ADP+SO4 - cow
1h8h - cATPase+ AMPPNP
1efr - cATPase+efrapeptin
3fks – ATPase – yeast
3ea0 – ATPase ParA, fragment – Chlorobium tepidum
2qen – ATPase (mutant) Walker-type – Pyrococcus abyssi
3cf0, 3cf1, 3cf3 – mATPase  NBD+ADP – mouse
3cf2 - mATPase NBD+ADP+AMP-PNP
2r31, 2p4x – PdATPase ATP12 – Paracoccus denitrificans
2zd2 – PdATPase (mutant) ATP12
1d8s – EcATPase F1
1vdz – ATPase subunit A – Pyrococcus horikoshii

Latest revision as of 14:36, 21 November 2024


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.

ATPase is inhibited by Bedaquiline which is used as TB drug[4].

For details see V-ATPase;

  • A-ATPase are found in archaea. For details see A-ATP Synthase;
  • P-ATPase transport ions[5]
  • E-ATPase hydrolyze extracellular ATP[6].
  • 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:



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

  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. ↑ Dupont C, Viljoen A, Thomas S, Roquet-Banères F, Herrmann JL, Pethe K, Kremer L. Bedaquiline Inhibits the ATP Synthase in Mycobacterium abscessus and Is Effective in Infected Zebrafish. Antimicrob Agents Chemother. 2017 Oct 24;61(11):e01225-17. PMID:28807917 doi:10.1128/AAC.01225-17
  5. ↑ 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
  6. ↑ 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
  7. ↑ Felix J, Bumba L, Liesche C, Fraudeau A, Rébeillé F, El Khoury JY, Huard K, Gallet B, Moriscot C, Kleman JP, Duhoo Y, Jessop M, Kandiah E, Barras F, Jouhet J, Gutsche I. The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane. Nat Commun. 2022 Sep 20;13(1):5502. PMID:36127320 doi:10.1038/s41467-022-32992-9
  8. ↑ Eichelberg K, Ginocchio CC, Galán JE. Molecular and functional characterization of the Salmonella typhimurium invasion genes invB and invC: homology of InvC to the F0F1 ATPase family of proteins. J Bacteriol. 1994 Aug;176(15):4501-10. PMID:8045880 doi:10.1128/jb.176.15.4501-4510.1994
  9. ↑ Rüttermann M, Koci M, Lill P, Geladas ED, Kaschani F, Klink BU, Erdmann R, Gatsogiannis C. Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate. Nat Commun. 2023 Sep 23;14(1):5942. PMID:37741838 doi:10.1038/s41467-023-41640-9
  10. ↑ Conaway RC, Conaway JW. The INO80 chromatin remodeling complex in transcription, replication and repair. Trends Biochem Sci. 2009 Feb;34(2):71-7. PMID:19062292 doi:10.1016/j.tibs.2008.10.010

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