6cu1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==X-ray structure of the S. typhimurium YrlA effector-binding module== | |||
<StructureSection load='6cu1' size='340' side='right' caption='[[6cu1]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6cu1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CU1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CU1 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></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=6cu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cu1 OCA], [http://pdbe.org/6cu1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cu1 RCSB], [http://www.ebi.ac.uk/pdbsum/6cu1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cu1 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Noncoding Y RNAs are present in both animal cells and many bacteria. In all species examined, Y RNAs tether the Ro60 protein to an effector protein to perform various cellular functions. Recently, a new Y RNA subfamily was identified in bacteria. Bioinformatic analyses of these YrlA (Y RNA-like A) RNAs predict that the effector-binding domain resembles tRNA. We present the structure of this domain, the overall folding of which is strikingly similar to canonical tRNAs. The tertiary interactions that are responsible for stabilizing tRNA are present in YrlA, making it a close tRNA mimic. However, YrlA lacks a free CCA end and contains a kink in the stem corresponding to the anticodon stem. Since nucleotides in the D and T stems are conserved among YrlAs, they may be an interaction site for an unknown factor. Our experiments identify YrlA RNAs as a new class of tRNA mimics. | |||
Structural Basis for tRNA Mimicry by a Bacterial Y RNA.,Wang W, Chen X, Wolin SL, Xiong Y Structure. 2018 Sep 27. pii: S0969-2126(18)30327-7. doi:, 10.1016/j.str.2018.09.001. PMID:30318468<ref>PMID:30318468</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6cu1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chen, X]] | |||
[[Category: Wang, W]] | |||
[[Category: Wolin, S L]] | |||
[[Category: Xiong, Y]] | |||
[[Category: Noncoding rna]] | |||
[[Category: Rna]] | |||
[[Category: Trna-like element]] | |||
[[Category: Y rna]] | |||
[[Category: Yrla]] | |||
Revision as of 09:49, 31 October 2018
X-ray structure of the S. typhimurium YrlA effector-binding moduleX-ray structure of the S. typhimurium YrlA effector-binding module
Structural highlights
Publication Abstract from PubMedNoncoding Y RNAs are present in both animal cells and many bacteria. In all species examined, Y RNAs tether the Ro60 protein to an effector protein to perform various cellular functions. Recently, a new Y RNA subfamily was identified in bacteria. Bioinformatic analyses of these YrlA (Y RNA-like A) RNAs predict that the effector-binding domain resembles tRNA. We present the structure of this domain, the overall folding of which is strikingly similar to canonical tRNAs. The tertiary interactions that are responsible for stabilizing tRNA are present in YrlA, making it a close tRNA mimic. However, YrlA lacks a free CCA end and contains a kink in the stem corresponding to the anticodon stem. Since nucleotides in the D and T stems are conserved among YrlAs, they may be an interaction site for an unknown factor. Our experiments identify YrlA RNAs as a new class of tRNA mimics. Structural Basis for tRNA Mimicry by a Bacterial Y RNA.,Wang W, Chen X, Wolin SL, Xiong Y Structure. 2018 Sep 27. pii: S0969-2126(18)30327-7. doi:, 10.1016/j.str.2018.09.001. PMID:30318468[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||