2vgm: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:2vgm.jpg|left|200px]]
{{Seed}}
[[Image:2vgm.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vgm|  PDB=2vgm  |  SCENE=  }}  
{{STRUCTURE_2vgm|  PDB=2vgm  |  SCENE=  }}  


'''STRUCTURE OF YEAST DOM34 : A PROTEIN RELATED TO TRANSLATION TERMINATION FACTOR ERF1 AND INVOLVED IN NO-GO DECAY.'''
===STRUCTURE OF YEAST DOM34 : A PROTEIN RELATED TO TRANSLATION TERMINATION FACTOR ERF1 AND INVOLVED IN NO-GO DECAY.===




==Overview==
<!--
The yeast protein Dom34 has been described to play a critical role in a newly identified mRNA decay pathway called No-Go decay. This pathway clears cells from mRNAs inducing translational stalls through endonucleolytic cleavage. Dom34 is related to the translation termination factor eRF1 and physically interacts with Hbs1, which is itself related to eRF3. We have solved the 2.5A resolution crystal structure of S. cerevisiae Dom34. This protein is organized in three domains with the central and C-terminal domains structurally homologous to those from eRF1. The N-terminal domain of Dom34 is different from eRF1. It adopts a Sm-fold which is often involved in the recognition of mRNA stem loops or in the recruitment of mRNA degradation machinery. The comparison of eRF1 and Dom34 domains proposed to interact directly with eRF3 and Hbs1, respectively, highlights striking structural similarities with eRF1 motifs identified to be crucial for the binding to eRF3. In addition, as observed for eRF1 which enhances eRF3 binding to GTP, the interaction of Dom34 with Hbs1 results in an increase in the affinity constant of Hbs1 for GTP but not GDP. Taken together, these results emphasize that eukaryotic cells have evolved two structurally related complexes able to interact with ribosomes either paused at a stop codon or stalled in translation by the presence of a stable stem-loop and to trigger ribosome release by catalyzing chemical bond hydrolysis.
The line below this paragraph, {{ABSTRACT_PUBMED_18180287}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18180287 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18180287}}


==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Translation regulation]]
[[Category: Translation regulation]]
[[Category: Translation termination factor]]
[[Category: Translation termination factor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:46:21 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:43:59 2008''

Revision as of 10:44, 29 July 2008

File:2vgm.png

Template:STRUCTURE 2vgm

STRUCTURE OF YEAST DOM34 : A PROTEIN RELATED TO TRANSLATION TERMINATION FACTOR ERF1 AND INVOLVED IN NO-GO DECAY.

Template:ABSTRACT PUBMED 18180287

About this Structure

2VGM is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure of yeast Dom34: a protein related to translation termination factor eRF1 and involved in No-Go decay., Graille M, Chaillet M, van Tilbeurgh H, J Biol Chem. 2008 Jan 7;. PMID:18180287

Page seeded by OCA on Tue Jul 29 13:43:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2vgm&oldid=743690"