The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA. - Wikidata - wikimedia - TriplyDB

The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA.

The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA.

http://www.wikidata.org/entity/Q44453265

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ABC transporters: the power to change Structure, function, and evolution of bacterial ATP-binding cassette systems The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter Stress Physiology of Lactic Acid Bacteria Ligand Binding and Crystal Structures of the Substrate-Binding Domain of the ABC Transporter OpuA Structural Insights into the Substrate Specificity of a 6-Phospho- -glucosidase BglA-2 from Streptococcus pneumoniae TIGR4 Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F X-ray structure of the Yersinia pestis heme transporter HmuUV Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F A novel flow cytometric HTS assay reveals functional modulators of ATP binding cassette transporter ABCB6 Catalytic and transport cycles of ABC exporters.The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter.Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases Engineering ecosystems and synthetic ecologies.Structural diversity of ABC transporters.The structures of MsbA: Insight into ABC transporter-mediated multidrug efflux.Transcriptome analysis reveals novel regulatory mechanisms in a genome-reduced bacterium.A sensor for intracellular ionic strength.Selective utilization of exogenous amino acids by Dehalococcoides ethenogenes strain 195 and its effects on growth and dechlorination activity Structural basis for substrate specificity of an amino acid ABC transporter.The ABCs of immunology: structure and function of TAP, the transporter associated with antigen processing.How do ABC transporters drive transport?The conformational coupling and translocation mechanism of vitamin B12 ATP-binding cassette transporter BtuCD.Two molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins.Uptake or extrusion: crystal structures of full ABC transporters suggest a common mechanism.Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis.CLC-0 and CFTR: chloride channels evolved from transporters.Review. Structure and mechanism of ATP-binding cassette transporters.Cost, effectiveness and environmental relevance of multidrug transporters in sea urchin embryos.Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.Bacterial ATP-driven transporters of transition metals: physiological roles, mechanisms of action, and roles in bacterial virulence.Sequential Action of MalE and Maltose Allows Coupling ATP Hydrolysis to Translocation in the MalFGK2 Transporter.The uncoupled ATPase activity of the ABC transporter BtuC2D2 leads to a hysteretic conformational change, conformational memory, and improved activity.Mechanistic diversity in ATP-binding cassette (ABC) transporters.Membrane protein reconstitution into giant unilamellar vesicles: a review on current techniques.On the role of the two extracytoplasmic substrate-binding domains in the ABC transporter OpuA.A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer.Physicochemical factors controlling the activity and energy coupling of an ionic strength-gated ATP-binding cassette (ABC) transporter.Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK(2)) from Escherichia coli/Salmonella during the transport cycle.Structural basis for binding and transfer of heme in bacterial heme-acquisition systems.

P2860

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P2860

The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA.

http://www.wikidata.org/entity/Q44453265

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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name

The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA.

@en

The ATP/substrate stoichiometry of the ATP-binding cassette

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type

label

The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA.

@en

The ATP/substrate stoichiometry of the ATP-binding cassette

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prefLabel

The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA.

@en

The ATP/substrate stoichiometry of the ATP-binding cassette

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Journal of Biological Chemistry

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The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA.

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P2093

Bert Poolman

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

Jason S Patzlaff

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Tiemen van der Heide

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport

On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine.

Characterization of the catalytic cycle of ATP hydrolysis by human P-glycoprotein. The two ATP hydrolysis events in a single catalytic cycle are kinetically similar but affect different functional outcomes.

A common mechanism for ATP hydrolysis in ABC transporter and helicase superfamilies.

Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport

Energy coupling to periplasmic binding protein-dependent transport systems: stoichiometry of ATP hydrolysis during transport in vivo

Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters

ABC transporters: one, two or four extracytoplasmic substrate-binding sites?

Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein.

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29546-29551

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scholarly article

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10.1074/JBC.M304796200

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32

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278

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2003-05-23T00:00:00Z

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12766159

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