Elongation factor Tu-targeted antibiotics: four different structures, two mechanisms of action (Q34552393)

3 August 2017

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title

Elongation factor Tu-targeted antibiotics: four different structures, two mechanisms of action (English)

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3 August 2017

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2

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3 August 2017

Andrea Parmeggiani

1

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PubMed ID

16876786

3 August 2017

language of work or name

English

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publication date

24 July 2006

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3 August 2017

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3 August 2017

580

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3 August 2017

19

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3 August 2017

4576-4581

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Mechanisms of EF-Tu, a pioneer GTPase

3 August 2017

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Crystal structure of active elongation factor Tu reveals major domain rearrangements

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

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

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

An alpha to beta conformational switch in EF-Tu

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Inhibitory mechanisms of antibiotics targeting elongation factor Tu.

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for development of novel antibiotics

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Substitution of histidine-84 and the GTPase mechanism of elongation factor Tu.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Effects of the antibiotic pulvomycin on the elongation factor Tu-dependent reactions. Comparison with other antibiotics

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Essential role of histidine 84 in elongation factor Tu for the chemical step of GTP hydrolysis on the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.07.039

10.1016/J.FEBSLET.2006.07.039

21 January 2018

Identifiers

DOI

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3 August 2017

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PubMed ID

16876786