2zy6: Difference between revisions
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==Crystal structure of a truncated tRNA, TPHE39A== | ==Crystal structure of a truncated tRNA, TPHE39A== | ||
<StructureSection load='2zy6' size='340' side='right' caption='[[2zy6]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='2zy6' size='340' side='right'caption='[[2zy6]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zy6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZY6 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2zy6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZY6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZY6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zy6 OCA], [http://pdbe.org/2zy6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zy6 RCSB], [http://www.ebi.ac.uk/pdbsum/2zy6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zy6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Kitago, Y]] | [[Category: Kitago, Y]] | ||
[[Category: Tanaka, I]] | [[Category: Tanaka, I]] | ||
Revision as of 15:11, 29 July 2020
Crystal structure of a truncated tRNA, TPHE39ACrystal structure of a truncated tRNA, TPHE39A
Structural highlights
Publication Abstract from PubMedThiI catalyzes the thio-introduction reaction to tRNA, and a truncated tRNA consisting of 39 nucleotides, TPHE39A, is the minimal RNA substrate for modification by ThiI from Escherichia coli. To examine the molecular basis of the tRNA recognition by ThiI, we have solved the crystal structure of TPHE39A, which showed that base pairs in the T-stem were almost completely disrupted, although those in the acceptor-stem were preserved. Gel shift assays and isothermal titration calorimetry experiments showed that ThiI can efficiently bind with not only tRNA(Phe) but also TPHE39A. Binding assays using truncated ThiI, i.e., N- and C-terminal domains of ThiI, showed that the N-domain can bind with both tRNA(Phe) and TPHE39A, whereas the C-domain cannot. These results indicated that the N-domain of ThiI recognizes the acceptor-stem region. Thermodynamic analysis indicated that the C-domain also affects RNA binding by its enthalpically favorable, but entropically unfavorable, contribution. In addition, circular dichroism spectra showed that the C-domain induced a conformation change in tRNA(Phe). Based on these results, a possible RNA binding mechanism of ThiI in which the N-terminal domain recognizes the acceptor-stem region and the C-terminal region causes a conformational change of RNA is proposed. Deduced RNA binding mechanism of ThiI based on structural and binding analyses of a minimal RNA ligand.,Tanaka Y, Yamagata S, Kitago Y, Yamada Y, Chimnaronk S, Yao M, Tanaka I RNA. 2009 Aug;15(8):1498-506. Epub 2009 Jun 9. PMID:19509301[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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