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Matches in DBpedia 2014 for { <http://dbpedia.org/resource/ATP_synthase_alpha/beta_subunits> ?p ?o. }

• beta_subunits abstract "ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport. F-ATPases (F1F0-ATPases) in mitochondria, chloroplasts and bacterial plasma membranes are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles, catalysing ATP hydrolysis to transport solutes and lower pH in organelles. A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases. P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes. E-ATPases are cell-surface enzymes that hydrolyse a range of nucleoside triphosphates, including extracellular ATP.The alpha and beta (or A and B) subunits are found in the F1, V1, and A1 complexes of F-, V- and A-ATPases, respectively, as well as flagellar ATPase and the termination factor Rho. The F-ATPases (or F1F0-ATPases), V-ATPases (or V1V0-ATPases) and A-ATPases (or A1A0-ATPases) are composed of two linked complexes: the F1, V1 or A1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the F0, V0 or A0 complex that forms the membrane-spanning pore. The F-, V- and A-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis.In F-ATPases, there are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex, while the remaining F1 subunits (gamma, delta, epsilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits, those on the beta subunits being catalytic, while those on the alpha subunits are regulatory. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP, which are induced by the rotation of the gamma subunit, itself is driven by the movement of protons through the F0 complex C subunit.In V- and A-ATPases, the alpha/A and beta/B subunits of the V1 or A1 complex are homologous to the alpha and beta subunits in the F1 complex of F-ATPases, except that the alpha subunit is catalytic and the beta subunit is regulatory.The alpha/A and beta/B subunits can each be divided into three regions, or domains, centred around the ATP-binding pocket, and based on structure and function. The central domain contains the nucleotide-binding residues that make direct contact with the ADP/ATP molecule.".
• beta_subunits symbol "ATP-synt_ab".
• beta_subunits symbol "ATP-synt_ab_C".
• beta_subunits symbol "ATP-synt_ab_N".
• beta_subunits thumbnail PBB_Protein_ATP5B_image.jpg?width=300.
• beta_subunits wikiPageID "14875994".
• beta_subunits wikiPageRevisionID "514381725".
• beta_subunits hasPhotoCollection beta_subunits.
• beta_subunits interpro "IPR000194".
• beta_subunits interpro "IPR000793".
• beta_subunits interpro "IPR004100".
• beta_subunits name "ATP synthase alpha/beta chain, C terminal domain".
• beta_subunits name "ATP synthase alpha/beta family, beta-barrel domain".
• beta_subunits name "ATP synthase alpha/beta family, nucleotide-binding domain".
• beta_subunits pdb "A:273-746 A:283-482 A:283-736 D:273-287 A:283-736 A:283-736 A:283-736 B:151-372 B:151-372 A:126-348 A:126-348 D:185-405 D:185-405 D:185-405 F:185-405 E:185-405 E:185-405 F:185-405 D:185-405 E:185-405 E:185-405 E:185-405 E:137-351 A:129-349 A:147-357 A:154-364".
• beta_subunits pdb "B:23-95 B:23-95 A:6-73 E:6-80 D:63-129 D:63-129 D:63-129 F:63-129 E:63-129 E:63-129 F:63-129 D:63-129 E:63-129 E:63-129 E:63-129 A:4-70 A:4-70 A:26-91 A:21-92".
• beta_subunits pdb "B:427-531 B:427-531 A:427-531 A:427-531 A:427-531 B:427-531 B:427-531 A:427-531 B:427-531 B:427-531 C:427-531 B:376-480 A:377-495 A:377-495 A:361-454 A:361-454 A:362-466".
• beta_subunits pfam "PF00006".
• beta_subunits pfam "PF00306".
• beta_subunits pfam "PF02874".
• beta_subunits prosite "PDOC00137".
• beta_subunits scop "1".
• beta_subunits symbol "ATP-synt_ab".
• beta_subunits symbol "ATP-synt_ab_C".
• beta_subunits symbol "ATP-synt_ab_N".
• beta_subunits subject Category:Protein_domains.
• beta_subunits subject Category:Protein_families.
• beta_subunits subject Category:Transmembrane_proteins.
• beta_subunits type Abstraction100002137.
• beta_subunits type Attribute100024264.
• beta_subunits type Chemical114806838.
• beta_subunits type Compound114818238.
• beta_subunits type Environment113934596.
• beta_subunits type Macromolecule114944888.
• beta_subunits type Material114580897.
• beta_subunits type Matter100020827.
• beta_subunits type Molecule114682133.
• beta_subunits type OrganicCompound114727670.
• beta_subunits type Part113809207.
• beta_subunits type PhysicalEntity100001930.
• beta_subunits type Protein114728724.
• beta_subunits type ProteinDomains.
• beta_subunits type Relation100031921.
• beta_subunits type Situation113927383.
• beta_subunits type Sphere114514039.
• beta_subunits type State100024720.
• beta_subunits type Substance100019613.
• beta_subunits type Thing100002452.
• beta_subunits type TransmembraneProteins.
• beta_subunits type Unit109465459.
• beta_subunits type Biomolecule.
• beta_subunits type Protein.
• beta_subunits type BiologicalObject.
• beta_subunits comment "ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient.".
• beta_subunits label "ATP synthase alpha/beta subunits".
• beta_subunits label "Subunidades alfa/beta da ATP sintase".
• beta_subunits sameAs beta_da_ATP_sintase.
• beta_subunits sameAs m.03g_wt7.
• beta_subunits sameAs Q4654885.
• beta_subunits sameAs Q4654885.
• beta_subunits sameAs beta_subunits.
• beta_subunits wasDerivedFrom beta_subunits?oldid=514381725.
• beta_subunits depiction PBB_Protein_ATP5B_image.jpg.
• beta_subunits isPrimaryTopicOf beta_subunits.