Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF - Test2 - elhamkhani - TriplyDB

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

http://www.wikidata.org/entity/Q27646943

about

Sequence co-evolution gives 3D contacts and structures of protein complexes ABC transporters: the power to change Structure, function, and evolution of bacterial ATP-binding cassette systems Structural insights into ABC transporter mechanism The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation Inter-domain communication mechanisms in an ABC importer: a molecular dynamics study of the MalFGK2E complex Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states 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 The Staphylococcus aureus Siderophore Receptor HtsA Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in an Arginine-rich Binding Pocket Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant Crystal structure of the maltose transporter in a pretranslocation intermediate state Insight into the Interaction of Metal Ions with TroA from Streptococcus suis Evidence for an allosteric mechanism of substrate release from membrane-transporter accessory binding proteins Arginine 116 stabilizes the entrance to the metal ion-binding site of the MntC protein An Asymmetry-to-Symmetry Switch in Signal Transmission by the Histidine Kinase Receptor for TMAO Asymmetric states of vitamin B₁₂ transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF Structures of Streptococcus pneumoniae PiaA and Its Complex with Ferrichrome Reveal Insights into the Substrate Binding and Release of High Affinity Iron Transporters Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F X-ray structure of the Yersinia pestis heme transporter HmuUV Structure of a bacterial energy-coupling factor transporter Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis Helicobacter pylori periplasmic receptor CeuE (HP1561) modulates its nickel affinity via organic metallophores Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F Ethanolamine activates a sensor histidine kinase regulating its utilization in Enterococcus faecalis Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8.Conformational flexibility of the leucine binding protein examined by protein domain coarse-grained molecular dynamics.The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB Structures of membrane proteins.Structural refinement of membrane proteins by restrained molecular dynamics and solvent accessibility data.Molecular models of human P-glycoprotein in two different catalytic states Probing the conformation of the resting state of a bacterial multidrug ABC transporter, BmrA, by a site-directed spin labeling approach Computational predictive models for P-glycoprotein inhibition of in-house chalcone derivatives and drug-bank compounds.Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes Solution NMR studies of periplasmic binding proteins and their interaction partners ArsAB, a novel enzyme from Sporomusa ovata activates phenolic bases for adenosylcobamide biosynthesis.A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation The conformational transition pathways of ATP-binding cassette transporter BtuCD revealed by targeted molecular dynamics simulation.Specificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus.

P2860

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P2860

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

http://www.wikidata.org/entity/Q27646943

description

2007 nî lūn-bûn

@nan

2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@ast

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@en

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@nl

type

label

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@ast

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@en

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@nl

prefLabel

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@ast

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@en

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@nl

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SCIENCE.1145950

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P1476

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF

@en

P2093

Birke A Goetz

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

Eduardo Perozo

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

Kaspar Hollenstein

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

Kaspar P Locher

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

Martina Niederer

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

Rikki N Hvorup

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P2860

H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB

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

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

Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding

The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter

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

An inward-facing conformation of a putative metal-chelate-type ABC transporter

Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP

Structure of an ABC transporter in complex with its binding protein

Structure of a bacterial multidrug ABC transporter

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1387-90

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scholarly article

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1237120

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10.1126/SCIENCE.1145950

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5843

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317

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2007-09-07T00:00:00Z

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17673622

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