Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter - Wikidata - wikimedia - TriplyDB

Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter

Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter

http://www.wikidata.org/entity/Q36861542

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Structural insights into ABC transporter mechanism Thermodynamics of ABC transporters Alternating Access in Maltose Transporter Mediated by Rigid-Body Rotations Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation Crystal structure of the maltose transporter in a pretranslocation intermediate state Snapshots of the maltose transporter during ATP hydrolysis Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography Structural basis for substrate specificity in the Escherichia coli maltose transport system The ATP-binding cassette transporter Cbc (choline/betaine/carnitine) recruits multiple substrate-binding proteins with strong specificity for distinct quaternary ammonium compounds Effects of lipid environment on the conformational changes of an ABC importer.Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2 Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment.A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation 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.Structural diversity of ABC transporters.Conformational coupling of the nucleotide-binding and the transmembrane domains in ABC transporters.Reaction chemistry ABC-style.The periplasmic membrane proximal domain of MacA acts as a switch in stimulation of ATP hydrolysis by MacB transporter.Transmembrane gate movements in the type II ATP-binding cassette (ABC) importer BtuCD-F during nucleotide cycle.Fructose uptake in Bifidobacterium longum NCC2705 is mediated by an ATP-binding cassette transporter.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.Two molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins.A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization.On the origin of large flexibility of P-glycoprotein in the inward-facing state Functionally important ATP binding and hydrolysis sites in Escherichia coli MsbA.EPR spectroscopy of MolB2C2-a reveals mechanism of transport for a bacterial type II molybdate importer Transmembrane signaling in the maltose ABC transporter MalFGK2-E: periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA.NMR and EPR studies of membrane transporters.Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.ABC transporters involved in export of cell surface glycoconjugates.Structure of ABC transporters.Molecular mechanism of the Escherichia coli maltose transporter.Diversity in ABC transporters: type I, II and III importers.Sequential Action of MalE and Maltose Allows Coupling ATP Hydrolysis to Translocation in the MalFGK2 Transporter.Active transporters as enzymes: an energetic framework applied to major facilitator superfamily and ABC importer systems.Allosteric transitions of the maltose transporter studied by an elastic network model.Maltose uptake by the novel ABC transport system MusEFGK2I causes increased expression of ptsG in Corynebacterium glutamicum.

P2860

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P2860

Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter

http://www.wikidata.org/entity/Q36861542

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

@zh-tw

2008年论文

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2008年论文

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2008年论文

@zh-cn

name

Both maltose-binding protein a ...... intact maltose ABC transporter

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type

label

Both maltose-binding protein a ...... intact maltose ABC transporter

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prefLabel

Both maltose-binding protein a ...... intact maltose ABC transporter

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P1433

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P356

PNAS.0803799105

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Both maltose-binding protein a ...... intact maltose ABC transporter

@en

P2093

Amy L Davidson

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

Candice S Klug

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Cedric Orelle

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R Michael Everly

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Tulin Ayvaz

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P2860

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

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

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

Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily

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

Formation of the productive ATP-Mg2+-bound dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus

Crystal structure of a catalytic intermediate of the maltose transporter

Role of glycine-534 and glycine-1179 of human multidrug resistance protein (MDR1) in drug-mediated control of ATP hydrolysis

Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations.

ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans.

P304

12837-12842

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P31

scholarly article

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10.1073/PNAS.0803799105

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P407

P433

35

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P478

105

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P577

2008-08-25T00:00:00Z

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P5875

23192416

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P698

18725638

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P932

2529024

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