Crystal structure of a mutant elongation factor G trapped with a GTP analogue (Q46637669)

23 December 2017

title

Crystal structure of a mutant elongation factor G trapped with a GTP analogue (English)

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23 December 2017

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5

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23 December 2017

author name string

Sebastian Hansson

1

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23 December 2017

Ranvir Singh

2

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23 December 2017

Anatoly T Gudkov

3

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23 December 2017

Anders Liljas

4

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23 December 2017

language of work or name

English

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publication date

1 August 2005

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23 December 2017

published in

FEBS Letters

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23 December 2017

volume

579

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23 December 2017

issue

20

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23 December 2017

page(s)

4492-4497

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23 December 2017

Comparison of guanosine triphosphate split and polypeptide synthesis with a purified E. coli system

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Ribosomes cannot interact simultaneously with elongation factors EF Tu and EF G.

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Elongation Factors EF Tu and EF G Interact at Related Sites on Ribosomes

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Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation

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Locking and unlocking of ribosomal motions

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Structural insights into fusidic acid resistance and sensitivity in EF-G.

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Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

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Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site

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

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X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding

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EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome

21 January 2018

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Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid

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Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs

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Crystal structure of active elongation factor Tu reveals major domain rearrangements

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

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Structure-function relationships in Escherichia coli translational elongation factor G: modification of lysine residues by the site-specific reagent pyridoxal phosphate.

21 January 2018

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Site-directed mutagenesis of the GDP binding domain of bacterial elongation factor Tu.

21 January 2018

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Classification and evolution of P-loop GTPases and related ATPases

21 January 2018

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The P-loop--a common motif in ATP- and GTP-binding proteins

21 January 2018

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Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha

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21 January 2018

Identifiers

DOI

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23 December 2017

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23 December 2017