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6q8v
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the standard kink turn HmKt-7 variant A2bm6A.== | |
| + | <StructureSection load='6q8v' size='340' side='right'caption='[[6q8v]], [[Resolution|resolution]] 2.09Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6q8v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q8V FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6MZ:N6-METHYLADENOSINE-5-MONOPHOSPHATE'>6MZ</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6q8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q8v OCA], [https://pdbe.org/6q8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q8v RCSB], [https://www.ebi.ac.uk/pdbsum/6q8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q8v ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | N(6)-methyladenine is the most common covalent modification in cellular RNA species, with demonstrated functional consequences. At the molecular level this methylation could alter local RNA structure, and/or modulate the binding of specific proteins. We have previously shown that trans-Hoogsteen-sugar (sheared) A:G base pairs can be completely disrupted by methylation, and that this occurs in a sub-set ofD/D k-turn structures. In this work we have investigated to what extent sequence context affects the severity with which inclusion of N(6)-methyladenine into different A:G base pairs of a standard k-turn affects RNA folding and L7Ae protein binding. We find that local sequence has a major influence, ranging from complete absence of folding and protein binding to a relatively mild effect. We have determined the crystal structure of one of these species both free and protein-bound, showing the environment of the methyl group and the way the modification is accommodated into the k-turn structure. | ||
| - | + | Effect of methylation of adenine N(6) on kink turn structure depends on location.,Ashraf S, Huang L, Lilley DMJ RNA Biol. 2019 Jun 24:1-9. doi: 10.1080/15476286.2019.1630797. PMID:31234702<ref>PMID:31234702</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6q8v" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Haloarcula marismortui]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Huang L]] | ||
| + | [[Category: Lilley DMJ]] | ||
Current revision
Structure of the standard kink turn HmKt-7 variant A2bm6A.
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