ATPase: Difference between revisions
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
<StructureSection load='RuvBL12_12mer.pdb' size='400' side='right' scene='Journal:JSB:1/Cv/2' caption='Human RuvB-like 1 dodecamer complex with ADP (PDB code [[2c9o]])'> | <StructureSection load='RuvBL12_12mer.pdb' size='400' side='right' scene='Journal:JSB:1/Cv/2' caption='Human RuvB-like 1 dodecamer complex with ADP (PDB code [[2c9o]])'> | ||
[[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. Vacuolar-type H+ ATPase (V-ATPase) couples the energy to proton transport across membranes. ATPAse types include: '''F-ATPase''' - the prime producers of ATP; '''V-ATPase''' transport solutes; '''A-ATPase''' are found in archaea; '''P-ATPase''' transport ions; '''E-ATPase''' hydrolyze extracellular ATP. Vacuolar-type H+ ATPase couples the energy to proton transport across membranes. 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:<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. Vacuolar-type H+ ATPase (V-ATPase) couples the energy to proton transport across membranes. ATPAse types include: '''F-ATPase''' - the prime producers of ATP; '''V-ATPase''' transport solutes; '''A-ATPase''' are found in archaea; '''P-ATPase''' transport ions; '''E-ATPase''' hydrolyze extracellular ATP. Vacuolar-type H+ ATPase couples the energy to proton transport across membranes. 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:<br /> | ||
| Line 18: | Line 18: | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of ATPase == | == 3D Structures of ATPase == | ||