6q8u
From Proteopedia
(Difference between revisions)
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<StructureSection load='6q8u' size='340' side='right'caption='[[6q8u]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='6q8u' size='340' side='right'caption='[[6q8u]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6q8u]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q8U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6q8u]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q8U FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=6MZ:N6-METHYLADENOSINE-5-MONOPHOSPHATE'>6MZ</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=6MZ:N6-METHYLADENOSINE-5-MONOPHOSPHATE'>6MZ</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpl7ae, AF_0764 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224325 ARCFU])</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=6q8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q8u OCA], [http://pdbe.org/6q8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q8u RCSB], [http://www.ebi.ac.uk/pdbsum/6q8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q8u ProSAT]</span></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=6q8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q8u OCA], [http://pdbe.org/6q8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q8u RCSB], [http://www.ebi.ac.uk/pdbsum/6q8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q8u ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RL7A_ARCFU RL7A_ARCFU]] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA and box C/D sRNAs.<ref>PMID:12560482</ref> | [[http://www.uniprot.org/uniprot/RL7A_ARCFU RL7A_ARCFU]] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA and box C/D sRNAs.<ref>PMID:12560482</ref> | ||
| + | <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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6q8u" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arcfu]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Huang, L]] | [[Category: Huang, L]] | ||
Revision as of 06:36, 10 July 2019
Structure of the standard kink turn HmKt-7 variant A2bm6A bound with AfL7Ae protein
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