A cryo-electron microscopic study of ribosome-bound termination factor RF2 (Q27640267)

8

0 references

Joachim Frank

9

Joachim Frank

0 references

Mikel Valle

4

Mikel Valle

0 references

Andrey V. Zavialov

Andrey V Zavialov

2

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Bente Vestergaard

Bente Vestergaard

7

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author name string

Urmila B S Rawat

1

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Jayati Sengupta

3

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Robert A Grassucci

5

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Jamie Linde

The structural basis of ribosome activity in peptide bond synthesis

6

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language of work or name

English

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publication date

2 January 2003

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published in

Nature

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volume

421

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issue

6918

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page(s)

87-90

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Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3.

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Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1

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A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3.

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A detailed view of a ribosomal active site: the structure of the L11-RNA complex

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Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition

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The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis

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Codon recognition in polypeptide chain termination: site directed crosslinking of termination codon to Escherichia coli release factor 2.

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Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution † 1 †This article is dedicated to the memory of Anneke van Heel. 1Edited by M.F. Moody

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Solution structure of the E. coli 70S ribosome at 11.5 A resolution

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The path of messenger RNA through the ribosome

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