2xl1: Difference between revisions
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[[ | ==STRUCTURAL BASIS OF TRANSLATIONAL STALLING BY HUMAN CYTOMEGALOVIRUS (HCMV) AND FUNGAL ARGININE ATTENUATOR PEPTIDE (AAP)== | ||
<StructureSection load='2xl1' size='340' side='right' caption='[[2xl1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xl1]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XL1 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xl1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xl1 RCSB], [http://www.ebi.ac.uk/pdbsum/2xl1 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Specific regulatory nascent chains establish direct interactions with the ribosomal tunnel, leading to translational stalling. Despite a wealth of biochemical data, structural insight into the mechanism of translational stalling in eukaryotes is still lacking. Here we use cryo-electron microscopy to visualize eukaryotic ribosomes stalled during the translation of two diverse regulatory peptides: the fungal arginine attenuator peptide (AAP) and the human cytomegalovirus (hCMV) gp48 upstream open reading frame 2 (uORF2). The C terminus of the AAP appears to be compacted adjacent to the peptidyl transferase center (PTC). Both nascent chains interact with ribosomal proteins L4 and L17 at tunnel constriction in a distinct fashion. Significant changes at the PTC were observed: the eukaryotic-specific loop of ribosomal protein L10e establishes direct contact with the CCA end of the peptidyl-tRNA (P-tRNA), which may be critical for silencing of the PTC during translational stalling. Our findings provide direct structural insight into two distinct eukaryotic stalling processes. | |||
Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide.,Bhushan S, Meyer H, Starosta AL, Becker T, Mielke T, Berninghausen O, Sattler M, Wilson DN, Beckmann R Mol Cell. 2010 Oct 8;40(1):138-46. PMID:20932481<ref>PMID:20932481</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Meyer, N H.]] | [[Category: Meyer, N H.]] | ||
[[Category: Sattler, M.]] | [[Category: Sattler, M.]] | ||
Revision as of 13:13, 22 October 2014
STRUCTURAL BASIS OF TRANSLATIONAL STALLING BY HUMAN CYTOMEGALOVIRUS (HCMV) AND FUNGAL ARGININE ATTENUATOR PEPTIDE (AAP)
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