3mjb: Difference between revisions
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< | ==Cricket Paralysis Virus IGR IRES Domain 3 RNA bound to sulfate== | ||
<StructureSection load='3mjb' size='340' side='right'caption='[[3mjb]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3mjb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MJB FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=3mjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mjb OCA], [https://pdbe.org/3mjb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mjb RCSB], [https://www.ebi.ac.uk/pdbsum/3mjb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mjb ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Although RNA molecules are highly negatively charged, anions have been observed bound to RNA in crystal structures. It has been proposed that anion binding sites found within isolated RNAs represent regions of the molecule that could be involved in intermolecular interactions, indicating potential contact points for negatively charged amino acids from proteins or phosphate groups from an RNA. Several types of anion binding sites have been cataloged based on available structures. However, currently there is no method for unambiguously assigning anions to crystallographic electron density, and this has precluded more detailed analysis of RNA-anion interaction motifs and their significance. We therefore soaked selenate into two different types of RNA crystals and used the anomalous signal from these anions to identify binding sites in these RNA molecules unambiguously. Examination of these sites and comparison with other suspected anion binding sites reveals features of anion binding motifs, and shows that selenate may be a useful tool for studying RNA-anion interactions. | |||
Identification and characterization of anion binding sites in RNA.,Kieft JS, Chase E, Costantino DA, Golden BL RNA. 2010 Jun;16(6):1118-23. Epub 2010 Apr 21. PMID:20410239<ref>PMID:20410239</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3mjb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Chase E]] | |||
[[Category: Costantino DA]] | |||
== | [[Category: Golden BL]] | ||
< | [[Category: Kieft JS]] | ||
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Latest revision as of 11:54, 6 September 2023
Cricket Paralysis Virus IGR IRES Domain 3 RNA bound to sulfateCricket Paralysis Virus IGR IRES Domain 3 RNA bound to sulfate
Structural highlights
Publication Abstract from PubMedAlthough RNA molecules are highly negatively charged, anions have been observed bound to RNA in crystal structures. It has been proposed that anion binding sites found within isolated RNAs represent regions of the molecule that could be involved in intermolecular interactions, indicating potential contact points for negatively charged amino acids from proteins or phosphate groups from an RNA. Several types of anion binding sites have been cataloged based on available structures. However, currently there is no method for unambiguously assigning anions to crystallographic electron density, and this has precluded more detailed analysis of RNA-anion interaction motifs and their significance. We therefore soaked selenate into two different types of RNA crystals and used the anomalous signal from these anions to identify binding sites in these RNA molecules unambiguously. Examination of these sites and comparison with other suspected anion binding sites reveals features of anion binding motifs, and shows that selenate may be a useful tool for studying RNA-anion interactions. Identification and characterization of anion binding sites in RNA.,Kieft JS, Chase E, Costantino DA, Golden BL RNA. 2010 Jun;16(6):1118-23. Epub 2010 Apr 21. PMID:20410239[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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