ATPase

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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:

  • F-ATPase - the prime producers of ATP;
  • V-ATPase or Vacuolar-type H+ ATPase couples the energy to proton transport across membranes;
  • A-ATPase are found in archaea. For details see A-ATP Synthase;
  • P-ATPase transport ions;
  • E-ATPase hydrolyze extracellular ATP.
  • 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)

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3D Structures of ATPase3D Structures of ATPase

Updated on 13-February-2016



  • The RuvBL1/RuvBL2 complex (ATPase)[1]'
    • Journal:JSB:1 - Structural and functional insights into a dodecameric molecular machine

ReferencesReferences

  1. Gorynia S, Bandeiras TM, Pinho FG, McVey CE, Vonrhein C, Round A, Svergun DI, Donner P, Matias PM, Carrondo MA. Structural and functional insights into a dodecameric molecular machine - The RuvBL1/RuvBL2 complex. J Struct Biol. 2011 Sep 10. PMID:21933716 doi:10.1016/j.jsb.2011.09.001

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