ATP synthase is an On the basis of a map at 32.5 Å resolution determined in situ in the mitochondria of the euglenozoan parasite, The anionic lipid cardiolipin is an essential component of active ATP synthases. FO F1 creates a pathway for protons movement across the membrane. enzyme that directly generates adenosine triphosphate (ATP) during the process of cellular respiration Mitochondrial ATP synthase. FO on the other hand has mainly hydrophobic regions.
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The best available structure to date is the one that we determined at 4 Å resolution in 2015 by X-ray crystallography of the enzyme complex from Relative to the extensive studies that we have carried out on mitochondrial enzymes, the structures of bacterial ATP synthases have been little investigated, except for structures of the FThe structures and functions of the components of ATP synthases, especially those subunits involved directly in the catalytic formation of ATP, are widely conserved in metazoans, fungi, eubacteria and plant chloroplasts. The other FThe binding change mechanism involves the active site of a β subunit's cycling between three states.The modular evolution theory for the origin of ATP synthase suggests that two subunits with independent function, a DNA helicase with ATPase activity and a A variety of natural and synthetic inhibitors of ATP synthase have been discovered.Yeast ATP synthase is one of the best-studied eukaryotic ATP synthases; and five FEukaryotes belonging to some divergent lineages have very special organizations of the ATP synthase. Annual Review of Biochemistry 66, 717-749. Located within the thylakoid membrane and the inner mitochondrial membrane, ATP synthase consists of two regions FO and F1. Other three subunits catalyze the ATP synthesis.
With the demethylated cUnderstanding the molecular mechanism of how ATP is made
FO causes rotation of F1 and is made of c-ring and subunits a, two b, F6. Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B.Abrahams JP, Buchanan SK, van Raaij MJ, Fearnley IM, Leslie AG & Walker JEThe structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin.Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism.Braig K, Menz RI, Montgomery MG, Leslie AG & Walker JEStructure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride.The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.The structure and nucleotide occupancy of bovine mitochondrial F(1)-ATPase are not influenced by crystallisation at high concentrations of nucleotide.Kagawa R, Montgomery MG, Braig K, Leslie AGW & Walker JEThe structure of bovine F1-ATPase inhibited by ADP and beryllium fluoride.How azide inhibits ATP hydrolysis by the F-ATPases.Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution.Watt IN, Montgomery MG, Runswick MJ, Leslie AGW & Walker JEBioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria.How release of phosphate from mammalian F1-ATPase generates a rotary substep.Molecular architecture of the rotary motor in ATP synthase.The structure of bovine F1-ATPase in complex with its regulatory protein IF1.Kabaleeswaran V, Puri N, Walker JE, Leslie AGW & Mueller DMNovel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria.Kabaleeswaran V, Shen H, Symersky J, Walker JE, Leslie AGW & Mueller DMAsymmetric structure of the yeast F1 ATPase in the absence of bound nucleotides.Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria.Robinson GC, Bason JV, Montgomery MG, Fearnley IM, Mueller DM, Leslie AGW & Walker JEThe structure of F₁-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF₁.Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F1-ATPase.Morales-Rios E, Montgomery MG, Leslie AGW & Walker JEStructure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.Zhou A, Rohou A, Schep DG, Bason JV, Montgomery MG, Walker JE, Grigorieff N & Rubinstein JLStructure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.Hahn A, Parey K, Bublitz M, Mills DJ, Zickermann V, Vonck J, Kühlbrandt W & Meier TStructure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology.Structure of the mitochondrial ATP synthase from Pichia angusta determined by electron cryo-microscopy.Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation.Shirakihara Y, Shiratori A, Tanikawa H, Nakasako M, Yoshida M & Suzuki TStructure of a thermophilic F1-ATPase inhibited by an ε-subunit: deeper insight into the ε-inhibition mechanism.Meier T, Polzer P, Diederichs K, Welte W & Dimroth PStructure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus.Matthies D, Preiss L, Klyszejko AL, Müller DJ, Cook GM, Vonck J & Meier TThe c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region.Preiss L, Langer JD, Yildiz Ö, Eckhardt-Strelau L, Guillemont JEG, Koul A & Meier TStructure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline.Ferguson SA, Cook GM, Montgomery MG, Leslie AGW & Walker JERegulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.Zhang AT, Montgomery MG, Leslie AGW, Cook GM & Walker JEThe structure of the catalytic domain of the ATP synthase from Mycobacterium smegmatis is a target for developing antitubercular drugs.Petri J, Nakatani Y, Montgomery MG, Ferguson SA, Aragão D, Leslie AGW, Heikal A, Walker JE & Cook GMStructure of F-ATPase from the obligate anaerobe Fusobacterium nucleatum.Sobti M, Smits C, Wong ASw, Ishmukhametov R, Stock D, Sandin S & Stewart AGCryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states.Mühleip AW, Dewar CE, Schnaufer A, Kühlbrandt W & Davies KMIn situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits.Gahura O, Šubrtová K, Váchová H, Panicucci B, Fearnley IM, Harbour ME, Walker JE & Zíková AThe F -ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18-subunit.Montgomery MG, Gahura O, Leslie AGW, Zíková A & Walker JEATP synthase fromhas an elaborated canonical F-domain and conventional catalytic sites.Pentatricopeptide repeat proteins in Trypanosoma brucei function in mitochondrial ribosomes.Cardiolipin binds selectively but transiently to conserved lysine residues in the rotor of metazoan ATP synthases.
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