Ion mobility-mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility.

Ion mobility-mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility.

Rotary ATPases play fundamental roles in energy conversion as their catalytic rotation is associated with interdomain fluctuations and heterogeneity of conformational states. Using ion mobility mass spectrometry we compared the conformational dynamics of the intact ATPase from Thermus thermophilus w...

Full description

Bibliographic Details
Main Authors:	Zhou, M, Politis, A, Davies, R, Liko, I, Wu, K, Stewart, A, Stock, D, Robinson, C
Format:	Journal article
Language:	English
Published:	2014

Similar Items

Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding.
by: Zhou, M, et al.
Published: (2011)

Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation
by: Schmidt, C, et al.
Published: (2013)

Cryo-EM reveals distinct conformations of E. coli ATP synthase on exposure to ATP
by: Sobti, M, et al.
Published: (2019)

Structural Modeling of Heteromeric Protein Complexes from Disassembly Pathways and Ion Mobility-Mass Spectrometry
by: Hall, Z, et al.
Published: (2012)

Structural modeling of heteromeric protein complexes from disassembly pathways and ion mobility-mass spectrometry.
by: Hall, Z, et al.
Published: (2012)

Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing.
by: Wang, S, et al.
Published: (2010)

Integrative modelling coupled with ion mobility mass spectrometry reveals structural features of the clamp loader in complex with single-stranded DNA binding protein
by: Politis, A, et al.
Published: (2013)

Integrative modelling coupled with ion mobility mass spectrometry reveals structural features of the clamp loader in complex with single-stranded DNA binding protein.
by: Politis, A, et al.
Published: (2013)

Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes.
by: Politis, A, et al.
Published: (2010)

Atomic insights of an up and down conformation of the Acinetobacter baumannii F₁-ATPase subunit ε and deciphering the residues critical for ATP hydrolysis inhibition and ATP synthesis
by: Saw, Wuan Geok, et al.
Published: (2023)

Probing conformations of amyloidogenic proteins by hydrogen exchange and mass spectrometry.
by: Nettleton, E, et al.
Published: (1999)

Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes.
by: Ruotolo, B, et al.
Published: (2007)

Protein folding and interactions revealed by mass spectrometry.
by: Last, A, et al.
Published: (1999)

Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry.
by: Gupta, S, et al.
Published: (2010)

Ion mobility-mass spectrometry reveals the influence of subunit packing and charge on the dissociation of multiprotein complexes.
by: Boeri Erba, E, et al.
Published: (2010)

Probing conformations of GroEL-bound substrate proteins by mass spectrometry.
by: Robinson, C, et al.
Published: (1998)

Flexible membrane proteins: functional dynamics captured by mass spectrometry.
by: Zhou, M, et al.
Published: (2014)

Mass spectrometry reveals differences in stability and subunit interactions between activated and nonactivated conformers of the (αβγδ)4 phosphorylase kinase complex.
by: Lane, L, et al.
Published: (2012)

Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III.
by: Lane, L, et al.
Published: (2011)

Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring.
by: van Duijn, E, et al.
Published: (2006)

Single-molecule visualization of conformational changes in the SecA ATPase
by: Sargent, Jacob D. (Jacob Daniel)
Published: (2015)

Cryo-EM reveals transition states of the Acinetobacter baumannii F1-ATPase rotary subunits γ and ε, unveiling novel compound targets
by: Le, Khoa Cong Minh, et al.
Published: (2025)

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.
by: Robinson, C, et al.
Published: (1994)

Ion imaging mass spectrometry
by: Yuen, W
Published: (2012)

Mass spectrometry guided structural biology.
by: Liko, I, et al.
Published: (2016)

Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies.
by: Benesch, J, et al.
Published: (2006)

Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies
by: Benesch, J, et al.
Published: (2006)

Mass spectrometry reveals synergistic effects of nucleotides, lipids, and drugs binding to a multidrug resistance efflux pump.
by: Marcoux, J, et al.
Published: (2013)

Ion mobility mass spectrometry of peptide ions: effects of drift gas and calibration strategies.
by: Bush, M, et al.
Published: (2012)

Mass spectrometry and ion molecule reactions /
by: 229486 Knewstubb, P. F.
Published: (1969)

The dependence on intracellular ATP concentration of ATP-sensitive K-channels and of Na,K-ATPase in intact HIT-T15 beta-cells.
by: Niki, I, et al.
Published: (1989)

EFFECTS OF VANADATE ON THE ATP CONTENT, ATPASE ACTIVITY AND PHOSPHATE ABSORPTION CAPACITY OF MAIZE ROOTS
by: Sklenar, J, et al.
Published: (1994)

Software requirements for the analysis and interpretation of native ion mobility mass spectrometry data
by: Allison, TM, et al.
Published: (2020)

Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA
by: Ariza, A, et al.
Published: (2005)

Ion mobility-mass spectrometry analysis of large protein complexes.
by: Ruotolo, B, et al.
Published: (2008)

Integrating mass spectrometry with MD simulations reveals the role of lipids in Na(+)/H(+) antiporters
by: Landreh, M, et al.
Published: (2017)

Ion mobility and molecular dynamics reveal charge-state dependent dissociation of protein complexes
by: Hall, Z, et al.
Published: (2012)

Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation.
by: Mancini, E, et al.
Published: (2004)

Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions.
by: Barrera, N, et al.
Published: (2009)

X-linked cholestasis in mouse due to mutations of the P4-ATPase ATP11C.
by: Siggs, O, et al.
Published: (2011)