3gca: Difference between revisions
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==The structural basis for recognition of the preQ0 metabolite by an unusually small riboswitch aptamer domain== | |||
<StructureSection load='3gca' size='340' side='right' caption='[[3gca]], [[Resolution|resolution]] 2.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3gca]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GCA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GCA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PQ0:2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDINE-5-CARBONITRILE'>PQ0</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3gca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gca OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gca RCSB], [http://www.ebi.ac.uk/pdbsum/3gca PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Riboswitches are RNA elements that control gene expression through metabolite binding. The preQ(1) riboswitch exhibits the smallest known ligand-binding domain and is of interest for its economical organization and high affinity interactions with guanine-derived metabolites required to confer tRNA wobbling. Here we present the crystal structure of a preQ(1) aptamer domain in complex with its precursor metabolite preQ(0). The structure is highly compact with a core that features a stem capped by a well organized decaloop. The metabolite is recognized within a deep pocket via Watson-Crick pairing with C15. Additional hydrogen bonds are made to invariant bases U6 and A29. The ligand-bound state confers continuous helical stacking throughout the core fold, thus providing a platform to promote Watson-Crick base pairing between C9 of the decaloop and the first base of the ribosome-binding site, G33. The structure offers insight into the mode of ribosome-binding site sequestration by a minimal RNA fold stabilized by metabolite binding and has implications for understanding the molecular basis by which bacterial genes are regulated. | |||
The structural basis for recognition of the PreQ0 metabolite by an unusually small riboswitch aptamer domain.,Spitale RC, Torelli AT, Krucinska J, Bandarian V, Wedekind JE J Biol Chem. 2009 Apr 24;284(17):11012-6. Epub 2009 Mar 4. PMID:19261617<ref>PMID:19261617</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Riboswitch|Riboswitch]] | *[[Riboswitch|Riboswitch]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: Spitale, R C | </StructureSection> | ||
[[Category: Wedekind, J E | [[Category: Spitale, R C]] | ||
[[Category: Wedekind, J E]] | |||
[[Category: Amptamer]] | [[Category: Amptamer]] | ||
[[Category: Metabolite]] | [[Category: Metabolite]] | ||
Revision as of 13:53, 17 December 2014
The structural basis for recognition of the preQ0 metabolite by an unusually small riboswitch aptamer domain
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