5mvq: Difference between revisions
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<StructureSection load='5mvq' size='340' side='right'caption='[[5mvq]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='5mvq' size='340' side='right'caption='[[5mvq]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5mvq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MVQ OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5mvq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MVQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.604Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5mvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mvq OCA], [https://pdbe.org/5mvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mvq RCSB], [https://www.ebi.ac.uk/pdbsum/5mvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mvq ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Brown T]] | ||
[[Category: | [[Category: Hardwick JS]] | ||
[[Category: | [[Category: Phillips SEV]] | ||
[[Category: | [[Category: Ptchelkine D]] | ||
Latest revision as of 20:51, 8 November 2023
Crystal structure of an unmodified, self-complementary dodecamer.Crystal structure of an unmodified, self-complementary dodecamer.
Structural highlights
Publication Abstract from PubMedThe mechanism by which the recently identified DNA modification 5-formylcytosine (fC) is recognized by epigenetic writer and reader proteins is not known. Recently, an unusual DNA structure, F-DNA, has been proposed as the basis for enzyme recognition of clusters of fC. We used NMR and X-ray crystallography to compare several modified DNA duplexes with unmodified analogs and found that in the crystal state the duplexes all belong to the A family, whereas in solution they are all members of the B family. We found that, contrary to previous findings, fC does not significantly affect the structure of DNA, although there are modest local differences at the modification sites. Hence, global conformation changes are unlikely to account for the recognition of this modified base, and our structural data favor a mechanism that operates at base-pair resolution for the recognition of fC by epigenome-modifying enzymes. 5-Formylcytosine does not change the global structure of DNA.,Hardwick JS, Ptchelkine D, El-Sagheer AH, Tear I, Singleton D, Phillips SEV, Lane AN, Brown T Nat Struct Mol Biol. 2017 May 15. doi: 10.1038/nsmb.3411. PMID:28504696[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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