Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation.
about
Sequence co-evolution gives 3D contacts and structures of protein complexesComparison between single-molecule and X-ray crystallography data on yeast F1-ATPaseGame on, science - how video game technology may help biologists tackle visualization challenges.Variations of Subunit of the Mycobacterium tuberculosis F1Fo ATP Synthase and a Novel Model for Mechanism of Action of the Tuberculosis Drug TMC207Crystal and NMR Structures Give Insights into the Role and Dynamics of Subunit F of the Eukaryotic V-ATPase from Saccharomyces cerevisiaeThe dynamic stator stalk of rotary ATPases.Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structuresElectron cryomicroscopy observation of rotational states in a eukaryotic V-ATPaseStructure of a thermophilic F1-ATPase inhibited by an ε-subunit: deeper insight into the ε-inhibition mechanismCryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational statesF1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurementsInhibition of F1-ATPase rotational catalysis by the carboxyl-terminal domain of the ϵ subunit.Single molecule optical measurements of orientation and rotations of biological macromoleculesF1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands.Binding of phytopolyphenol piceatannol disrupts β/γ subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATPase.Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor.Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation.The binary protein-protein interaction landscape of Escherichia coliSpecific evolution of F1-like ATPases in mycoplasmas.The regulatory switch of F1-ATPase studied by single-molecule FRET in the ABEL Trap.The torque of rotary F-ATPase can unfold subunit gamma if rotor and stator are cross-linked.Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.ε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition.The beta subunit loop that couples catalysis and rotation in ATP synthase has a critical length.Thymoquinone Inhibits Escherichia coli ATP Synthase and Cell Growth.I-COMS: Interprotein-COrrelated Mutations ServerCell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membraneAerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase.Purification, characterization and crystallization of the F-ATPase from Paracoccus denitrificansStructure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.Improved crystallization of Escherichia coli ATP synthase catalytic complex (F1) by introducing a phosphomimetic mutation in subunit ε.The structural basis of a high affinity ATP binding ε subunit from a bacterial ATP synthase.Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein.Structural Plasticity of the Protein Plug That Traps Newly Packaged Genomes in Podoviridae Virions.Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry.Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarumTwisting and subunit rotation in single F(O)(F1)-ATP synthase.Microscopy of single F(o) F(1) -ATP synthases--the unraveling of motors, gears, and controls.pH-dependent regulation of electron transport and ATP synthesis in chloroplasts.Spotlighting motors and controls of single FoF1-ATP synthase.
P2860
Q21128770-EA97200E-4382-4138-B8E6-35663E03DAD9Q27309090-38DC49DA-6968-4CC3-B854-73EE5F972A7EQ27336073-805F394F-38DC-4578-AE0A-13FB2CF5AAE5Q27674675-CDCADD96-6357-45F9-95E0-2F0722A1A5B4Q27676743-55F7EC43-0DCE-4CF5-B97B-BCB49869EC1AQ27677401-863D8D55-C33C-4059-BA47-E0FC2F720E8AQ27683798-6C3A9950-B704-4ED2-939C-6CD13EF6A6DFQ27700838-1B5193CD-611D-41F1-9B48-5AFF6B642446Q27700948-FAB08CAD-D6F4-4699-A2AA-5AF7887D1F20Q28818044-B15CDB4B-E97D-4B76-8C9A-BCBDF3C1650EQ28829498-EE74DAE4-61FF-4ADC-A6C1-A6F24834D5B6Q30366884-68458389-6A18-4B72-94B1-BAF8B154DFE2Q30398533-A0CBBD42-C3E6-4F21-A58B-445C82F78D93Q30414148-ED4D1A31-5C36-4B9F-9B5A-9875B62C7740Q30418606-CC827E63-1AC3-4AA4-9B56-E091A283CEA9Q30827472-C0FF3EBF-A8F5-4511-9B28-93D46E7260AFQ30837348-AC88902F-8C5D-4DB7-9251-0BEC14ABD24AQ34010755-C05B8231-6C2B-49BD-9B02-44D3575EB305Q34299752-3D88FBDF-8740-4519-9CC2-32A246EAB80AQ34303885-60EEDAF6-93D9-4682-8D43-92CA12D6A026Q34542610-90A1D48E-2BF6-4B7A-8B38-7CC391206EB8Q34631137-42700166-9740-4EDA-B486-431F5D2732FDQ34965697-4C7AF61B-15BF-44EB-96EE-A7394C1217B1Q35313850-7CEB5ACB-633C-4F5A-88B9-2D21BDC42F17Q35634052-FC8BBA98-2139-4D52-9CE8-E524A3DE16CBQ35810199-F08996C0-BFC1-4E11-A15D-03BB7D8D825CQ35884527-12BECEC9-D960-4224-8B1E-697430EC635FQ35978276-A9634CEB-7B3F-4C3B-B001-98B75543EBC5Q36122269-AE189FD6-0A7C-414A-AE18-C50AA9C4A233Q36238412-ED8A1725-AFB8-469A-BAF0-596BC26D6AC8Q36375635-6B84EE0B-1280-45CB-A806-F923EE599CA8Q36380751-6DB2A0AF-D78F-4FE5-93D5-1B3C5EC7508EQ36389592-F4069F93-6854-44E0-B932-E2E996CEF8B8Q36419241-FC61AACC-A035-4D46-99DC-B426CEDF67E7Q36658989-698EA2CF-CC27-44CC-B059-1418C0D2BA03Q37304887-A55686D9-8CE8-41E6-A0A6-7F32039E5921Q38069810-2B1D7ECC-1DEA-42C2-9EBC-835AF00295E0Q38078891-A3E50D31-136A-435A-A6EB-7B60368CC885Q38108529-78F311E9-CD8B-4DCF-A8C0-450113920E67Q38141066-BE588C8F-15FF-4689-A400-BA5682A5AF1F
P2860
Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Structure of the ATP synthase ...... an autoinhibited conformation.
@ast
Structure of the ATP synthase ...... an autoinhibited conformation.
@en
Structure of the ATP synthase catalytic complex
@nl
type
label
Structure of the ATP synthase ...... an autoinhibited conformation.
@ast
Structure of the ATP synthase ...... an autoinhibited conformation.
@en
Structure of the ATP synthase catalytic complex
@nl
prefLabel
Structure of the ATP synthase ...... an autoinhibited conformation.
@ast
Structure of the ATP synthase ...... an autoinhibited conformation.
@en
Structure of the ATP synthase catalytic complex
@nl
P2860
P356
P1476
Structure of the ATP synthase ...... an autoinhibited conformation.
@en
P2093
Gino Cingolani
Thomas M Duncan
P2860
P2888
P304
P356
10.1038/NSMB.2058
P577
2011-05-22T00:00:00Z