2cky: Difference between revisions
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[[ | ==STRUCTURE OF THE ARABIDOPSIS THALIANA THIAMINE PYROPHOSPHATE RIBOSWITCH WITH ITS REGULATORY LIGAND== | ||
<StructureSection load='2cky' size='340' side='right' caption='[[2cky]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2cky]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CKY FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OS:OSMIUM+ION'>OS</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene><br> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cky OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cky RCSB], [http://www.ebi.ac.uk/pdbsum/2cky PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Riboswitches are untranslated regions of messenger RNA, which adopt alternate structures depending on the binding of specific metabolites. Such conformational switching regulates the expression of proteins involved in the biosynthesis of riboswitch substrates. Here, we present the 2.9 angstrom-resolution crystal structure of the eukaryotic Arabidopsis thaliana thiamine pyrophosphate (TPP)-specific riboswitch in complex with its natural ligand. The riboswitch specifically recognizes the TPP via conserved residues located within two highly distorted parallel "sensor" helices. The structure provides the basis for understanding the reorganization of the riboswitch fold upon TPP binding and explains the mechanism of resistance to the antibiotic pyrithiamine. | |||
Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand.,Thore S, Leibundgut M, Ban N Science. 2006 May 26;312(5777):1208-11. Epub 2006 May 4. PMID:16675665<ref>PMID:16675665</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Ban, N.]] | [[Category: Ban, N.]] | ||
[[Category: Leibundgut, M.]] | [[Category: Leibundgut, M.]] | ||
[[Category: Thore, S.]] | [[Category: Thore, S.]] | ||
[[Category: Nucleic acid]] | [[Category: Nucleic acid]] | ||
Revision as of 06:39, 29 September 2014
STRUCTURE OF THE ARABIDOPSIS THALIANA THIAMINE PYROPHOSPHATE RIBOSWITCH WITH ITS REGULATORY LIGANDSTRUCTURE OF THE ARABIDOPSIS THALIANA THIAMINE PYROPHOSPHATE RIBOSWITCH WITH ITS REGULATORY LIGAND
Structural highlights
Publication Abstract from PubMedRiboswitches are untranslated regions of messenger RNA, which adopt alternate structures depending on the binding of specific metabolites. Such conformational switching regulates the expression of proteins involved in the biosynthesis of riboswitch substrates. Here, we present the 2.9 angstrom-resolution crystal structure of the eukaryotic Arabidopsis thaliana thiamine pyrophosphate (TPP)-specific riboswitch in complex with its natural ligand. The riboswitch specifically recognizes the TPP via conserved residues located within two highly distorted parallel "sensor" helices. The structure provides the basis for understanding the reorganization of the riboswitch fold upon TPP binding and explains the mechanism of resistance to the antibiotic pyrithiamine. Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand.,Thore S, Leibundgut M, Ban N Science. 2006 May 26;312(5777):1208-11. Epub 2006 May 4. PMID:16675665[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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