H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB - Wikidata - thesis-toulmin - TriplyDB

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

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

http://www.wikidata.org/entity/Q24529132

about

ABC transporters: the power to change Structure, function, and evolution of bacterial ATP-binding cassette systems The ABC protein turned chloride channel whose failure causes cystic fibrosis Flexibility in the ABC transporter MsbA: Alternating access with a twist.Mammalian P4-ATPases and ABC transporters and their role in phospholipid transport Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF Molecular Dynamism of Fe–S Cluster Biosynthesis Implicated by the Structure of the SufC2–SufD2 Complex Insights into How Nucleotide-Binding Domains Power ABC Transport Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant P. aeruginosa PilT Structures with and without Nucleotide Reveal a Dynamic Type IV Pilus Retraction Motor Aromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPase Snapshots of the maltose transporter during ATP hydrolysis Kinetics of the Association/Dissociation Cycle of an ATP-binding Cassette Nucleotide-binding Domain Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states Asymmetric states of vitamin B₁₂ transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF The ABC-F protein EttA gates ribosome entry into the translation elongation cycle Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F Tel1 and Rif2 Regulate MRX Functions in End-Tethering and Repair of DNA Double-Strand Breaks Transporter engineering for improved tolerance against alkane biofuels in Saccharomyces cerevisiae Energy transduction and alternating access of the mammalian ABC transporter P-glycoprotein.Stabilization of Nucleotide Binding Domain Dimers Rescues ABCC6 Mutants Associated with Pseudoxanthoma Elasticum.Structural consequences of ATP hydrolysis on the ABC transporter NBD dimer: molecular dynamics studies of HlyB.Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter.The DrrAB efflux system of Streptomyces peucetius is a multidrug transporter of broad substrate specificity Asymmetric switching in a homodimeric ABC transporter: a simulation study CFTR and TNR-CFTR expression and function in the kidney.The conformational transition pathway of ATP binding cassette transporter MsbA revealed by atomistic simulations.Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysis The H-loop in the second nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator is required for efficient chloride channel closing Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel Potentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs.Conserved allosteric hot spots in the transmembrane domains of cystic fibrosis transmembrane conductance regulator (CFTR) channels and multidrug resistance protein (MRP) pumps.The A-loop, a novel conserved aromatic acid subdomain upstream of the Walker A motif in ABC transporters, is critical for ATP binding.The response of Lactococcus lactis to membrane protein production Defective lipid transport and biosynthesis in recessive and dominant Stargardt macular degeneration An interaction between the Walker A and D-loop motifs is critical to ATP hydrolysis and cooperativity in bacteriophage T4 Rad50 The hydroxyl group of S685 in Walker A motif and the carboxyl group of D792 in Walker B motif of NBD1 play a crucial role for multidrug resistance protein folding and function.ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation

P2860

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P2860

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

http://www.wikidata.org/entity/Q24529132

description

2005 nî lūn-bûn

@nan

2005 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2005年の論文

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2005年論文

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2005年論文

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2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

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name

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@ast

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@en

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@en-gb

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@nl

type

label

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@ast

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@en

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@en-gb

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@nl

prefLabel

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@ast

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@en

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@en-gb

H662 is the linchpin of ATP hy ...... in of the ABC transporter HlyB

@nl

P1433

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SJ.EMBOJ.7600657

P1433

The EMBO Journal

P1476

H662 is the linchpin of ATP hy ...... n of the ABC transporter HlyB.

@en

P2093

I Barry Holland

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

Jelena Zaitseva

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

Lutz Schmitt

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

Stefan Jenewein

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

Thorsten Jumpertz

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

P2860

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

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

Substrate-assisted catalysis: molecular basis and biological significance

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7

Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export

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

Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter

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

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1901-1910

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scholarly article

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3576681

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10.1038/SJ.EMBOJ.7600657

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11

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24

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2005-05-12T00:00:00Z

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7852457

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15889153

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1142601

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