Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.
about
Cryo-EM studies of the structure and dynamics of vacuolar-type ATPasesRotating with the brakes on and other unresolved features of the vacuolar ATPaseModels for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covarianceCryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational statesThe changing landscape of membrane protein structural biology through developments in electron microscopy.Oscillating Electric Field Measures the Rotation Rate in a Native Rotary EnzymeIdentification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the Fo-a subunit of Propionigenium modestum ATP synthasePurification, characterization and crystallization of the F-ATPase from Paracoccus denitrificansBiophysical comparison of ATP-driven proton pumping mechanisms suggests a kinetic advantage for the rotary process depending on coupling ratio.Integrating macromolecular X-ray diffraction data with the graphical user interface iMosflm.Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry.Cardiolipin binds selectively but transiently to conserved lysine residues in the rotor of metazoan ATP synthases.Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarumBiophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process.A modular platform for one-step assembly of multi-component membrane systems by fusion of charged proteoliposomes.Identification of G8969>A in mitochondrial ATP6 gene that severely compromises ATP synthase function in a patient with IgA nephropathy.Structure of the mitochondrial ATP synthase from Pichia angusta determined by electron cryo-microscopyStructure and mechanism of the ATP synthase membrane motor inferred from quantitative integrative modeling.Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase.Protonation-dependent stepped rotation of the F-type ATP synthase c-ring observed by single-molecule measurements.Catalytic robustness and torque generation of the F1-ATPasePurification of Ovine Respiratory Complex I Results in a Highly Active and Stable Preparation.Molecular architecture of the N-type ATPase rotor ring from Burkholderia pseudomallei.Respiratory Complex I in Bos taurus and Paracoccus denitrificans Pumps Four Protons across the Membrane for Every NADH Oxidized.Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane MorphologyEngineering a light-controlled F1 ATPase using structure-based protein design.Atomic model for the membrane-embedded VO motor of a eukaryotic V-ATPase.Biophysical Characterization of a Thermoalkaliphilic Molecular Motor with a High Stepping Torque Gives Insight into Evolutionary ATP Synthase Adaptation.Structural basis of proton translocation and force generation in mitochondrial ATP synthase.Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.Deleting the IF1-like ζ subunit from Paracoccus denitrificans ATP synthase is not sufficient to activate ATP hydrolysis.ATP synthase from Trypanosoma brucei has an elaborated canonical F1-domain and conventional catalytic sites.Deletion of a unique loop in the mycobacterial F-ATP synthase γ subunit sheds light on its inhibitory role in ATP hydrolysis-driven H(+) pumping.Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase.Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.ATP Synthase Diseases of Mitochondrial Genetic Origin.Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopyThe Peripheral Stalk of Rotary ATPases
P2860
Q26741088-99727BB0-30DD-42C4-9149-404484003CC3Q26747183-DC21DECE-FBD9-42A7-A2CB-0E1D623C5225Q27316939-3D4016AE-A75C-4004-912A-4A53E3E1D562Q28818044-4A5CF86A-369A-4A8D-BC36-43F89ABD586FQ30392684-18BB0DF9-FE11-4D0A-B0EC-91D35EF249B8Q30842923-2A3DD5BA-2884-4BD1-96C6-703A31A4C605Q33738049-133C494A-C97B-41C5-B886-A81326517149Q36122269-F3831173-2E29-4F8E-988C-A8A94007A64BQ36314842-ED0BD153-EB5B-4F16-94FE-3FDF594DE87CQ36388988-0CDD51FF-F1D6-499D-BF8B-255519E9CD20Q36658989-6BB28CE7-CAF1-4DD8-B918-FC2C89BEFA20Q37161637-AEFD257C-3F2C-4625-9E83-6BE965B46672Q37304887-DD0D4C12-4411-4898-A329-AE527D66FB1CQ37322964-698BC371-45CE-4209-B195-F67479FCC70FQ37330426-2CF3F812-9EAE-491C-8DD6-4E1656F4B5EAQ37393858-A31CCB5C-52FA-4E75-A076-701A9D543CB2Q37417752-D2D6E20C-1072-4811-A000-50452796CBCBQ37457022-A13B16C4-0A62-48C8-A4A0-15A29835245FQ37737116-32FFB5BB-7ADF-4BFE-BBC0-9C44F2FFBC36Q38607687-419BBA4E-34A2-497A-9E8A-D12E27885864Q39251244-6D5062A9-EAB8-434C-ABD9-49E7C19DC799Q39348089-05369C49-9BE2-43DB-9D38-B3F501746C6FQ40298749-E849819A-4548-4B3F-B733-AD6B238C71FFQ42293000-FF598DF6-0F38-4E56-8446-90A3B395A456Q42365237-875E72FC-6E80-408C-B746-863CB8E7928BQ42379356-3E808E51-DA6E-463F-8143-87D488B9D653Q45045809-F0CF4AC5-3E79-40B5-97DF-7E4960AA4A97Q46052720-313D7FE5-1BF1-44DD-8CD9-4AEC2D8688C3Q47133960-5685EC60-7F91-4B28-931A-0B9B4E958CDCQ47213682-ABC533C4-34C5-4648-B4BB-74D6AADF1462Q48043961-ABDC5688-3C7C-4D40-A534-E223BF0DB74EQ50026439-1AFF6CC1-41B9-4627-BB43-0F7FD3D44139Q50688127-4378D7B1-044F-4FE0-B685-F42D5BAEE140Q51197632-1C90D181-955D-4B33-8004-AE43AA7165DDQ53819039-DCE4343F-7E0B-4ED5-9D12-889FB98E4230Q55355374-F16E5321-E05D-496C-8116-5C2C0E3D0718Q57799810-13F22ADC-03F0-4134-8EC6-9451D9BBD7D6Q58764725-CF893DA7-CEF9-4F68-98DE-4793C2990CC3
P2860
Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Structure of ATP synthase from ...... llography at 4.0 Å resolution.
@ast
Structure of ATP synthase from ...... llography at 4.0 Å resolution.
@en
type
label
Structure of ATP synthase from ...... llography at 4.0 Å resolution.
@ast
Structure of ATP synthase from ...... llography at 4.0 Å resolution.
@en
prefLabel
Structure of ATP synthase from ...... llography at 4.0 Å resolution.
@ast
Structure of ATP synthase from ...... llography at 4.0 Å resolution.
@en
P2860
P50
P356
P1476
Structure of ATP synthase from ...... llography at 4.0 Å resolution.
@en
P2093
Andrew G W Leslie
P2860
P304
13231-13236
P356
10.1073/PNAS.1517542112
P407
P577
2015-10-12T00:00:00Z