Atp synthase

• Article • • 10 August 2021 Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase • • • • • • ORCID: orcid.org/0000-0002-3935-6907 • • ORCID: orcid.org/0000-0003-4522-3008 • • • … • ORCID: orcid.org/0000-0001-9187-3736 Show authors Nature Communications volume 12, Article number: 4835 ( 2021) F-ATP synthase is a leading candidate as the mitochondrial permeability transition pore (PTP) but the mechanism(s) leading to channel formation remain undefined. Here, to shed light on the structural requirements for PTP formation, we test cells ablated for g, OSCP and b subunits, and ρ 0 cells lacking subunits a and A6L. Δg cells (that also lack subunit e) do not show PTP channel opening in intact cells or patch-clamped mitoplasts unless atractylate is added. Δb and ΔOSCP cells display currents insensitive to cyclosporin A but inhibited by bongkrekate, suggesting that the adenine nucleotide translocator (ANT) can contribute to channel formation in the absence of an assembled F-ATP synthase. Mitoplasts from ρ 0 mitochondria display PTP currents indistinguishable from their wild-type counterparts. In this work, we show that peripheral stalk subunits are essential to turn the F-ATP synthase into the PTP and that the ANT provides mitochondria with a distinct permeability pathway. The permeability transition (PT) is a Ca 2+-dependent permeability increase of the mitochondrial inner membrane to ions and solutes with m...

ATP Synthase The ATP synthase is a mitochondrial enzyme localized in the inner membrane, where it catalyzes the synthesis of ATP from ADP and phosphate, driven by a flux of protons across a gradient generated by electron transfer from the proton chemically positive to the negative side. From: Autoantibodies (Second Edition), 2007 Related terms: • Electron Transport Chain • Adenosine Diphosphate • Mitochondrial DNA • Adenosine Triphosphate • Mitochondrion • Oxidative Phosphorylation • Brain • Electron Transport • Inner Membrane • Mitochondrial Membrane David G. Whitehouse, ... Anthony L. Moore, in Reference Module in Biomedical Sciences, 2019 The ATP Synthase The ATP synthase (or F 1F 0 ATPase and also referred to as complex V) uses the free energy of an electrochemical gradient of protons (or sodium ions) generated by the respiratory chain to synthesize ATP. The ATP synthases comprise a very large group of highly conserved enzymes that are found in the bacterial cytoplasmic membranes, the thylakoid membranes of chloroplasts, and the inner membranes of mitochondria. Most members of the group use H + as the coupling ion (the Propionigenium modestum enzyme is an example of the few ATP synthases that can use Na + as the physiological coupling ion). G. Schäfer, in Encyclopedia of Biological Chemistry (Second Edition), 2013 Secondary Energy Transducers ATP synthetases (⇒) are the most important universal secondary energy transducers integrated into plasma membranes. Bacterial AT...

• العربية • Bosanski • Čeština • Deutsch • Eesti • Español • فارسی • Français • Galego • 한국어 • Italiano • ქართული • Latina • Lietuvių • Македонски • Nederlands • 日本語 • Polski • Português • Русский • Slovenčina • Српски / srpski • Srpskohrvatski / српскохрватски • Suomi • Українська • Tiếng Việt • 中文 +/K +ATPase Transmembrane ATPases import metabolites necessary for +/K +ATPase) that maintains the +/K +ATPase or gastric proton pump) that acidifies the contents of the stomach. ATPase is genetically conserved in animals; therefore, Besides exchangers, other categories of transmembrane ATPase include +/K +ATPase, cause a net flow of charge, but others do not. These are called electrogenic transporters and electroneutral transporters, respectively. "The membrane-bound copper transporting adenosine triphosphatase (Cu-ATPase), which selectively binds copper ions, transports copper ions into and out of cells (Harris et al. 1998)." Source: Structure [ ] The Mechanism [ ] ATPase (also called F 0F 1-ATP Synthase) is a charge-transferring complex that catalyzes ATP to perform ATP synthesis by moving ions through the membrane. The coupling of ATP hydrolysis and transport is a chemical reaction in which a fixed number of solute molecules are transported for each ATP molecule hydrolyzed; for the Na +/K + exchanger, this is three Na + ions out of the cell and two K+ ions inside per ATP molecule hydrolyzed. Transmembrane ATPases make use of ATP's chemical potential energy by performing mec...

MT-ATP6 and MT-ATP6 (in blue) or in the +1 frame for MT-ATP8 (in red). MT-ATP6 (or ATP6) is a ATP synthase F o subunit 6 (or subunit/chain A). This subunit belongs to the F o complex of the large, transmembrane F-type MT-ATP6 gene have been found in approximately 10 to 20 percent of people with Structure [ ] MT-ATP6 gene on the L strand of the human mitochondrial genome. MT-ATP6 is one of the two ATP synthase mitochondrial genes (red boxes). The MT-ATP6 gene provides information for making a protein that is essential for normal mitochondrial function. The human MT-ATP6 gene, located in MT-ATP6 is the 46- MT-ATP6 reading frame (+3), the MT-ATP8 gene ends in the +1 reading frame with a TAG The MT-ATP6 protein weighs 24.8 kDa and is composed of 226 1F o ATPase, also known as o portion of the complex. The 1 fraction derives its name from the term "Fraction 1" and F o (written as a subscript letter "o", not "zero") derives its name from being the binding fraction for o unit of ATP synthase. o region of ATP synthase is a proton pore that is embedded in the mitochondrial membrane. It consists of three main subunits A, B, and C, and (in humans) six additional subunits, Function [ ] This subunit is a key component of the proton channel, and may play a direct role in the translocation of protons across the membrane. Catalysis in the F 1 complex depends upon the rotation of the central stalk and F o c-ring, which in turn is driven by the flux of protons through the membrane via the i...

• Article • • 05 January 2021 ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria • ORCID: orcid.org/0000-0002-1877-2282 • ORCID: orcid.org/0000-0002-4918-6438 • • • ORCID: orcid.org/0000-0003-2651-1215 • ORCID: orcid.org/0000-0001-5909-2307 • … • ORCID: orcid.org/0000-0002-5302-1740 Show authors Nature Communications volume 12, Article number: 120 ( 2021) Mitochondrial ATP synthase plays a key role in inducing membrane curvature to establish cristae. In Apicomplexa causing diseases such as malaria and toxoplasmosis, an unusual cristae morphology has been observed, but its structural basis is unknown. Here, we report that the apicomplexan ATP synthase assembles into cyclic hexamers, essential to shape their distinct cristae. Cryo-EM was used to determine the structure of the hexamer, which is held together by interactions between parasite-specific subunits in the lumenal region. Overall, we identified 17 apicomplexan-specific subunits, and a minimal and nuclear-encoded subunit -a. The hexamer consists of three dimers with an extensive dimer interface that includes bound cardiolipins and the inhibitor IF 1. Cryo-ET and subtomogram averaging revealed that hexamers arrange into ~20-megadalton pentagonal pyramids in the curved apical membrane regions. Knockout of the linker protein ATPTG11 resulted in the loss of pentagonal pyramids with concomitant aberrantly shaped cristae. Together, this demonstrates that the unique macromolecular arrangement is critica...

• Article • • 10 August 2021 Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase • • • • • • ORCID: orcid.org/0000-0002-3935-6907 • • ORCID: orcid.org/0000-0003-4522-3008 • • • … • ORCID: orcid.org/0000-0001-9187-3736 Show authors Nature Communications volume 12, Article number: 4835 ( 2021) F-ATP synthase is a leading candidate as the mitochondrial permeability transition pore (PTP) but the mechanism(s) leading to channel formation remain undefined. Here, to shed light on the structural requirements for PTP formation, we test cells ablated for g, OSCP and b subunits, and ρ 0 cells lacking subunits a and A6L. Δg cells (that also lack subunit e) do not show PTP channel opening in intact cells or patch-clamped mitoplasts unless atractylate is added. Δb and ΔOSCP cells display currents insensitive to cyclosporin A but inhibited by bongkrekate, suggesting that the adenine nucleotide translocator (ANT) can contribute to channel formation in the absence of an assembled F-ATP synthase. Mitoplasts from ρ 0 mitochondria display PTP currents indistinguishable from their wild-type counterparts. In this work, we show that peripheral stalk subunits are essential to turn the F-ATP synthase into the PTP and that the ANT provides mitochondria with a distinct permeability pathway. The permeability transition (PT) is a Ca 2+-dependent permeability increase of the mitochondrial inner membrane to ions and solutes with m...

MT-ATP6 and MT-ATP6 (in blue) or in the +1 frame for MT-ATP8 (in red). MT-ATP6 (or ATP6) is a ATP synthase F o subunit 6 (or subunit/chain A). This subunit belongs to the F o complex of the large, transmembrane F-type MT-ATP6 gene have been found in approximately 10 to 20 percent of people with Structure [ ] MT-ATP6 gene on the L strand of the human mitochondrial genome. MT-ATP6 is one of the two ATP synthase mitochondrial genes (red boxes). The MT-ATP6 gene provides information for making a protein that is essential for normal mitochondrial function. The human MT-ATP6 gene, located in MT-ATP6 is the 46- MT-ATP6 reading frame (+3), the MT-ATP8 gene ends in the +1 reading frame with a TAG The MT-ATP6 protein weighs 24.8 kDa and is composed of 226 1F o ATPase, also known as o portion of the complex. The 1 fraction derives its name from the term "Fraction 1" and F o (written as a subscript letter "o", not "zero") derives its name from being the binding fraction for o unit of ATP synthase. o region of ATP synthase is a proton pore that is embedded in the mitochondrial membrane. It consists of three main subunits A, B, and C, and (in humans) six additional subunits, Function [ ] This subunit is a key component of the proton channel, and may play a direct role in the translocation of protons across the membrane. Catalysis in the F 1 complex depends upon the rotation of the central stalk and F o c-ring, which in turn is driven by the flux of protons through the membrane via the i...

• العربية • Bosanski • Čeština • Deutsch • Eesti • Español • فارسی • Français • Galego • 한국어 • Italiano • ქართული • Latina • Lietuvių • Македонски • Nederlands • 日本語 • Polski • Português • Русский • Slovenčina • Српски / srpski • Srpskohrvatski / српскохрватски • Suomi • Українська • Tiếng Việt • 中文 +/K +ATPase Transmembrane ATPases import metabolites necessary for +/K +ATPase) that maintains the +/K +ATPase or gastric proton pump) that acidifies the contents of the stomach. ATPase is genetically conserved in animals; therefore, Besides exchangers, other categories of transmembrane ATPase include +/K +ATPase, cause a net flow of charge, but others do not. These are called electrogenic transporters and electroneutral transporters, respectively. "The membrane-bound copper transporting adenosine triphosphatase (Cu-ATPase), which selectively binds copper ions, transports copper ions into and out of cells (Harris et al. 1998)." Source: Structure [ ] The Mechanism [ ] ATPase (also called F 0F 1-ATP Synthase) is a charge-transferring complex that catalyzes ATP to perform ATP synthesis by moving ions through the membrane. The coupling of ATP hydrolysis and transport is a chemical reaction in which a fixed number of solute molecules are transported for each ATP molecule hydrolyzed; for the Na +/K + exchanger, this is three Na + ions out of the cell and two K+ ions inside per ATP molecule hydrolyzed. Transmembrane ATPases make use of ATP's chemical potential energy by performing mec...

• Article • • 05 January 2021 ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria • ORCID: orcid.org/0000-0002-1877-2282 • ORCID: orcid.org/0000-0002-4918-6438 • • • ORCID: orcid.org/0000-0003-2651-1215 • ORCID: orcid.org/0000-0001-5909-2307 • … • ORCID: orcid.org/0000-0002-5302-1740 Show authors Nature Communications volume 12, Article number: 120 ( 2021) Mitochondrial ATP synthase plays a key role in inducing membrane curvature to establish cristae. In Apicomplexa causing diseases such as malaria and toxoplasmosis, an unusual cristae morphology has been observed, but its structural basis is unknown. Here, we report that the apicomplexan ATP synthase assembles into cyclic hexamers, essential to shape their distinct cristae. Cryo-EM was used to determine the structure of the hexamer, which is held together by interactions between parasite-specific subunits in the lumenal region. Overall, we identified 17 apicomplexan-specific subunits, and a minimal and nuclear-encoded subunit -a. The hexamer consists of three dimers with an extensive dimer interface that includes bound cardiolipins and the inhibitor IF 1. Cryo-ET and subtomogram averaging revealed that hexamers arrange into ~20-megadalton pentagonal pyramids in the curved apical membrane regions. Knockout of the linker protein ATPTG11 resulted in the loss of pentagonal pyramids with concomitant aberrantly shaped cristae. Together, this demonstrates that the unique macromolecular arrangement is critica...

ATP Synthase The ATP synthase is a mitochondrial enzyme localized in the inner membrane, where it catalyzes the synthesis of ATP from ADP and phosphate, driven by a flux of protons across a gradient generated by electron transfer from the proton chemically positive to the negative side. From: Autoantibodies (Second Edition), 2007 Related terms: • Electron Transport Chain • Adenosine Diphosphate • Mitochondrial DNA • Adenosine Triphosphate • Mitochondrion • Oxidative Phosphorylation • Brain • Electron Transport • Inner Membrane • Mitochondrial Membrane David G. Whitehouse, ... Anthony L. Moore, in Reference Module in Biomedical Sciences, 2019 The ATP Synthase The ATP synthase (or F 1F 0 ATPase and also referred to as complex V) uses the free energy of an electrochemical gradient of protons (or sodium ions) generated by the respiratory chain to synthesize ATP. The ATP synthases comprise a very large group of highly conserved enzymes that are found in the bacterial cytoplasmic membranes, the thylakoid membranes of chloroplasts, and the inner membranes of mitochondria. Most members of the group use H + as the coupling ion (the Propionigenium modestum enzyme is an example of the few ATP synthases that can use Na + as the physiological coupling ion). G. Schäfer, in Encyclopedia of Biological Chemistry (Second Edition), 2013 Secondary Energy Transducers ATP synthetases (⇒) are the most important universal secondary energy transducers integrated into plasma membranes. Bacterial AT...