NDLI: Molecular Morphology of Eukaryotic Class-1 Translation Termination Factor eRF1 in Solution

Content Provider	Springer Nature Link
Author	Konenko, A. V. Dembo, K. A. Kisselev, L. L. Volkov, V. V.
Copyright Year	2004
Abstract	The integral structural parameters and the shape of the molecule of human translation termination factor eRF1 were determined from the small-angle X-ray scattering in solution. The molecular shapes were found by bead modeling with nonlinear minimization of the root-mean-square deviation of the calculated from the experimental scattering curve. Comparisons of the small-angle scattering curves computed for atomic-resolution structures of eRF1 with the experimental data on scattering from solution testified that the crystal and the solution conformations are close. In the ribosome, the distance between the eRF1 motifs GGQ and NIKS must be shorter than in crystal or solution (75 versus 100–107 Å). Therefore, like its bacterial counterpart RF2, the eukaryotic eRF1 must change its conformation as it binds to the ribosome. The conformational mobility of eukaryotic and prokaryotic class-1 release factors is another feature making them functionally akin to tRNA.
Starting Page	253
Ending Page	260
Page Count	8
File Format	PDF
ISSN	00268933
Journal	Molecular Biology
Volume Number	38
Issue Number	2
e-ISSN	16083245
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2004-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Human Genetics Life Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biophysics

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Thermal denaturation of class 1 eukaryotic translation termination factor eRF1. Relationship between stability and functional activity of eRF1 mutants

Model of the structure of the eukaryotic ribosomal translation termination complex

How does Euplotes translation termination factor eRF1 fail to recognize the UGA stop codon?

Translation termination factor eRF1 of the ciliate Blepharisma japonicum recognizes all three stop codons

Interface of the interaction of the middle domain of human translation termination factor eRF1 with eukaryotic ribosomes

A New Method to Measure the Functional Activity of Class-1 Translation Termination Factor eRF1

Influence of individual domains of the translation termination factor eRF1 on induction of the GTPase activity of the translation termination factor eRF3

Nonstandard genetic codes and translation termination

Increased tRNA level in yeast cells with mutant translation termination factors eRF1 and eRF3

Molecular Morphology of Eukaryotic Class-1 Translation Termination Factor eRF1 in Solution

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Translation termination factor eRF1 of the ciliate Blepharisma japonicum recognizes all three stop codons

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