Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis (Q27653327)

9

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Poul Nissen

8

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Klaus Schulten

10

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Joachim Frank

11

object named as

Joachim Frank

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Elizabeth Villa

1

object named as

Elizabeth Villa

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author name string

Jayati Sengupta

2

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Leonardo G Trabuco

3

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Jamie LeBarron

4

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William T Baxter

5

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Tanvir R Shaikh

6

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Robert A Grassucci

Proceedings of the National Academy of Sciences of the United States of America

7

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language of work or name

English

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publication date

27 January 2009

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published in

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volume

106

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issue

4

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page(s)

1063-8

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cites work

Visualization of the eEF2–80S Ribosome Transition-State Complex by Cryo-Electron Microscopy

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

20 March 2017

1 reference

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Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex

20 March 2017

1 reference

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Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process

20 March 2017

1 reference

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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

20 March 2017

1 reference

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Structure of the GDP-Pi complex of Gly203-->Ala gialpha1: a mimic of the ternary product complex of galpha-catalyzed GTP hydrolysis

20 March 2017

1 reference

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An alpha to beta conformational switch in EF-Tu

20 March 2017

1 reference

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

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613361

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

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613361

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

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613361

VMD: visual molecular dynamics

20 March 2017

1 reference

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The guanine nucleotide-binding switch in three dimensions

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613361

Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics

20 March 2017

1 reference

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Dynamics of Recognition between tRNA and elongation factor Tu

7 April 2017

1 reference

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Preparation of macromolecular complexes for cryo-electron microscopy

29 September 2017

1 reference

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Structural basis for mRNA and tRNA positioning on the ribosome

29 September 2017

1 reference

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Functional conformations of the L11-ribosomal RNA complex revealed by correlative analysis of cryo-EM and molecular dynamics simulations

29 September 2017

1 reference

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Structural insights into translational fidelity

29 September 2017

1 reference

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Intact aminoacyl-tRNA is required to trigger GTP hydrolysis by elongation factor Tu on the ribosome

29 September 2017

1 reference

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The ribosome-in-pieces: binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA.

29 September 2017

1 reference

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Crystal structure of active elongation factor Tu reveals major domain rearrangements

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613361

Characterization of the GTPase reaction of elongation factor Tu. Determination of the stereochemical course in the presence of antibiotic X5108

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613361

Exploration of parameters in cryo-EM leading to an improved density map of the E. coli ribosome

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613361

Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2613361

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

2 June 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0811370106

The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0811370106

A pathway for the transmission of allosteric signals in the ribosome through a network of RNA tertiary interactions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0811370106

tRNA selection and kinetic proofreading in translation

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0811370106

Limited proteolysis and amino acid replacements in the effector region of Thermus thermophilus elongation factor Tu.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0811370106

The importance of structural transitions of the switch II region for the functions of elongation factor Tu on the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0811370106

Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0811370106

GTPase activation of elongation factors Tu and G on the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0811370106

An A to U transversion at position 1067 of 23 S rRNA from Escherichia coli impairs EF-Tu and EF-G function 1 1Edited by D. E. Draper

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19122150

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.0811370106

1 reference

ADS bibcode

2009PNAS..106.1063V

0 references

1 reference

1 reference

PubMed publication ID

19122150

1 reference