Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox - Wikidata - thesis-toulmin - TriplyDB

Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox

Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox

http://www.wikidata.org/entity/Q27630920

about

Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu tRNAs as antibiotic targets An open conformation of the Thermus thermophilus gyrase B ATP-binding domain Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis GTPase activation of elongation factor EF-Tu by the ribosome during decoding.The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA The Mechanism for Activation of GTP Hydrolysis on the Ribosome Identifying ligand-binding hot spots in proteins using brominated fragments An interbacterial NAD(P)(+) glycohydrolase toxin requires elongation factor Tu for delivery to target cells Ternatin and improved synthetic variants kill cancer cells by targeting the elongation factor-1A ternary complex.Antibiotics: where to throw the spanner in the ribosomal machinery?The process of mRNA-tRNA translocation Identification of novel inhibitors of bacterial translation elongation factors Finding biologically relevant protein domain interactions: conserved binding mode analysis Phenelfamycins G and H, new elfamycin-type antibiotics produced by Streptomyces albospinus Acta 3619.The function and synthesis of ribosomes.Elongation factor Tu-targeted antibiotics: four different structures, two mechanisms of action.Cofactor dependent conformational switching of GTPases.Elongation factor Ts directly facilitates the formation and disassembly of the Escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex.Mechanism of the chemical step for the guanosine triphosphate (GTP) hydrolysis catalyzed by elongation factor Tu Functional effects of deleting the coiled-coil motif in Escherichia coli elongation factor Ts.Elfamycins: inhibitors of elongation factor-Tu.Biosynthesis of polyketides by trans-AT polyketide synthases.The unique tuf2 gene from the kirromycin producer Streptomyces ramocissimus encodes a minor and kirromycin-sensitive elongation factor Tu.Polyketide Bioderivatization Using the Promiscuous Acyltransferase KirCII.A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation.An unusual mechanism for EF-Tu activation during tmRNA-mediated ribosome rescue.Molecular dynamics of ribosomal elongation factors G and Tu.Elongation factor Tu3 (EF-Tu3) from the kirromycin producer Streptomyces ramocissimus Is resistant to three classes of EF-Tu-specific inhibitors.tRNA selection and kinetic proofreading in translation.The kirromycin gene cluster of Streptomyces collinus Tü 365 codes for an aspartate-alpha-decarboxylase, KirD, which is involved in the biosynthesis of the precursor beta-alanine.Antibiotic susceptibility of mammalian mitochondrial translation.Inhibitors or toxins? Large library target-specific screening of fullerene-based nanoparticles for drug design purpose.Filling the Gaps in the Kirromycin Biosynthesis: Deciphering the Role of Genes Involved in Ethylmalonyl-CoA Supply and Tailoring Reactions.E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form The transorientation hypothesis for codon recognition during protein synthesis

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Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox

http://www.wikidata.org/entity/Q27630920

description

2001 nî lūn-bûn

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2001 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2001 թվականի մայիսին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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Conformational change of elong ...... between EF-Tu.GDP and aurodox

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G J Palm

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J R Mesters

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L Vogeley

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R Hilgenfeld

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P2860

The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

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

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA

Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: atomic basis for GE2270A inhibition of EF-Tu

Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog

The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation

The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution

Helix unwinding in the effector region of elongation factor EF-Tu-GDP

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10.1074/JBC.M100017200

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20

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276

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crystal structure