Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport. - Wikidata - wikimedia - TriplyDB

Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport.

Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport.

http://www.wikidata.org/entity/Q38341900

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Structure, function, and evolution of bacterial ATP-binding cassette systems Structural insights into ABC transporter mechanism Thermodynamics of ABC transporters Alternating Access in Maltose Transporter Mediated by Rigid-Body Rotations Studies of the Maltose Transport System Reveal a Mechanism for Coupling ATP Hydrolysis to Substrate Translocation without Direct Recognition of Substrate Apo and ligand-bound structures of ModA from the archaeonMethanosarcina acetivorans Snapshots of the maltose transporter during ATP hydrolysis Structural basis for substrate specificity in the Escherichia coli maltose transport system Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2 Probing the conformation of the resting state of a bacterial multidrug ABC transporter, BmrA, by a site-directed spin labeling approach Stimulation of the maltose transporter ATPase by unliganded maltose binding protein A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation Dipolar coupling between nitroxide spin labels: the development and application of a tether-in-a-cone model.Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporter Uncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter.In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.How do ABC transporters drive transport?Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter Conformational plasticity of the type I maltose ABC importer.Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle.NMR and EPR studies of membrane transporters.Molecular mechanism of the Escherichia coli maltose transporter.Diversity in ABC transporters: type I, II and III importers.Active transporters as enzymes: an energetic framework applied to major facilitator superfamily and ABC importer systems.ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2).ATP alone triggers the outward facing conformation of the maltose ATP-binding cassette transporter.A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein.Binding Protein-Dependent Uptake of Maltose into Cells via an ATP-Binding Cassette Transporter.The interplay between effector binding and allostery in an engineered protein switch.Probing receptor-translocator interactions in the oligopeptide ABC transporter by fluorescence correlation spectroscopy.Characterization of the LSGGQ and H motifs from the Escherichia coli lipid A transporter MsbA CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains.One intact transmembrane substrate binding site is sufficient for function of the homodimeric type I ATP-binding cassette importer for positively charged amino acids Art(MP)2 of Geobacillus stearothermophilus.Conformational dynamics in binding-protein-independent mutant of the Escherichia coli maltose transporter, MalG511 and its interaction with maltose binding protein.

P2860

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P2860

Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport.

http://www.wikidata.org/entity/Q38341900

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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2004年學術文章

@zh-hant

name

Maltose-binding protein is ope ...... ysis during maltose transport.

@en

type

label

Maltose-binding protein is ope ...... ysis during maltose transport.

@en

prefLabel

Maltose-binding protein is ope ...... ysis during maltose transport.

@en

P1433

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P2860

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P356

P1433

Journal of Biological Chemistry

P1476

Maltose-binding protein is ope ...... ysis during maltose transport.

@en

P2093

Amy L Davidson

http://www.w3.org/2001/XMLSchema#string

Candice S Klug

http://www.w3.org/2001/XMLSchema#string

Jason A Hall

http://www.w3.org/2001/XMLSchema#string

Mariana I Austermuhle

http://www.w3.org/2001/XMLSchema#string

P2860

Vanadate-catalyzed photocleavage of the signature motif of an ATP-binding cassette (ABC) transporter.

Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle

Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters

The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter

The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism

Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis

A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle

X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution

Crystal structure of the ATP-binding subunit of an ABC transporter

The human ATP-binding cassette (ABC) transporter superfamily

P304

28243-28250

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scholarly article

P356

10.1074/JBC.M403508200

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P407

P433

27

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P478

279

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P577

2004-04-26T00:00:00Z

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P698

15117946

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