SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction. - Wikidata - awgldk - TriplyDB

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

http://www.wikidata.org/entity/Q37399396

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Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane The Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor Lipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein Targeting The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins.Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.Ribosome-SRP-FtsY cotranslational targeting complex in the closed state The subcellular distribution of an RNA quality control protein, the Ro autoantigen, is regulated by noncoding Y RNA binding.A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway Breaking on through to the other side: protein export through the bacterial Sec system.Signal recognition particle: an essential protein-targeting machine.Co-translational protein targeting to the bacterial membrane.Fidelity of cotranslational protein targeting by the signal recognition particle.Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting.Signal sequences activate the catalytic switch of SRP RNA.Substrate binding disrupts dimerization and induces nucleotide exchange of the chloroplast GTPase Toc33.Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity.The bacterial SRP receptor, FtsY, is activated on binding to the translocon.Membrane proteins take center stage in Frankfurt.The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon

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P2860

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

http://www.wikidata.org/entity/Q37399396

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on September 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

@en

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

@nl

type

label

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

@en

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

@nl

prefLabel

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

@en

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

@nl

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Nature Structural & Molecular Biology

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SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

@en

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John D Gross

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

Niels Bradshaw

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

Peter Walter

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

Saskia B Neher

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

Stephen N Floor

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

P2860

X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates

GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation

Prediction of signal recognition particle RNA genes.

The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting

Mechanism of association and reciprocal activation of two GTPases

Crystal structure of the ribonucleoprotein core of the signal recognition particle

Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY

X-ray structure of the T. Aquaticus Ftsy:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases

Substrate twinning activates the signal recognition particle and its receptor

Heterodimeric GTPase Core of the SRP Targeting Complex

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916-923

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scholarly article

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10.1038/NSMB.1467

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9

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15

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2008-09-01T00:00:00Z

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23951871

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1001402423

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19172744

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2767265

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