ATPase: Difference between revisions
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[[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. ATPase types include:<br /> | [[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. 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.--> | * '''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. For details see [[V-ATPase]];<br /> | * '''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<ref>PMID:28807917</ref>. | |||
For details see [[V-ATPase]];<br /> | |||
* '''A-ATPase''' are found in archaea. For details see [[A-ATP Synthase]];<br /> | * '''A-ATPase''' are found in archaea. For details see [[A-ATP Synthase]];<br /> | ||
* '''P-ATPase''' transport ions | * '''P-ATPase''' transport ions<ref>PMID:20962537</ref><br /> | ||
* '''E-ATPase''' hydrolyze extracellular ATP. <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 /> | * '''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 domains include metal-binding domain (MBD) and nucleotide-binding domain (NBD). For more details see:<br /> | ||
*Cu transporting ATPase are in [[P(1B)-Type Cu(I) Transporting ATPases ATP7A and ATP7B]].<br /> | * '''ATPase RavA''' participates in the pathway which response to ahminoglycosides under anaerobic conditions and cell membrane regulation<ref>PMID:36127320</ref>. <br /> | ||
*Na/K transporting ATPase are in [[Sodium-Potassium ATPase]].<br /> | * '''ATPase InvC''' energizes the apparatus needed for the entry of ''Salmonella typhimurium'' into mammalian cells<ref>PMID:8045880</ref>. <br /> | ||
*H/K transporting ATPase are in [[Esomeprazole and H+/K+ - ATPase Interaction]].<br /> | * '''Peroxisomal ATPase''' Pex1/Pex6 is essential for peroxisome formation<ref>PMID:37741838</ref>. <br /> | ||
*Transitional endoplasmic reticulum ATPase are in [[Valosin Containing Protein D120]].<br /> | * '''INO8o ATPase''' is a component of the chromatin remodelling complex<ref>PMID:19062292</ref>. <br /> | ||
*Central stalk in F(1)-ATPase is described in [[A-ATP Synthase]]<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 /> | *[[Journal:JSB:1|RuvBL1/RuvBL2 complex (ATPase)]]<br /> | ||
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
[[Category:3D printer files]] | |||
Latest revision as of 14:29, 28 November 2025
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3D 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 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 ATPase
References
Proteopedia Page Contributors and Editors (what is this?)
Alexander Berchansky, Mark Hoelzer, Marius Mihasan, Jaime Prilusky, Karsten Theis, Michal Harel, Wayne Decatur
