7r77
From Proteopedia
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| - | ==== | + | ==Cryo-EM structure of DNMT5 binary complex with hemimethylated DNA== |
| - | <StructureSection load='7r77' size='340' side='right'caption='[[7r77]]' scene=''> | + | <StructureSection load='7r77' size='340' side='right'caption='[[7r77]], [[Resolution|resolution]] 3.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7r77]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptococcus_neoformans Cryptococcus neoformans] and [https://en.wikipedia.org/wiki/Cryptococcus_neoformans_var._grubii_H99 Cryptococcus neoformans var. grubii H99]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R77 FirstGlance]. <br> |
| - | </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=7r77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r77 OCA], [https://pdbe.org/7r77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r77 RCSB], [https://www.ebi.ac.uk/pdbsum/7r77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r77 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7r77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r77 OCA], [https://pdbe.org/7r77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r77 RCSB], [https://www.ebi.ac.uk/pdbsum/7r77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r77 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DMT5_CRYNH DMT5_CRYNH] ATP-dependent cytosine methylase that maintains DNA methylation by acting at hemimethylated palindromic 5'-CG-3' sites to produce symmetrically methylated DNA strands (PubMed:24630728, PubMed:31955845, PubMed:32437639). DNA methylation may play a role in transcriptional silencing, particularly at transposable elements (PubMed:24630728).<ref>PMID:24630728</ref> <ref>PMID:31955845</ref> <ref>PMID:32437639</ref> <ref>PMID:24630728</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Epigenetic evolution occurs over million-year timescales in Cryptococcus neoformans and is mediated by DNMT5, the first maintenance type cytosine methyltransferase identified in the fungal or protist kingdoms, the first dependent on adenosine triphosphate (ATP), and the most hemimethyl-DNA-specific enzyme known. To understand these novel properties, we solved cryo-EM structures of CnDNMT5 in three states. These studies reveal an elaborate allosteric cascade in which hemimethylated DNA binding first activates the SNF2 ATPase domain by a large rigid body rotation while the target cytosine partially flips out of the DNA duplex. ATP binding then triggers striking structural reconfigurations of the methyltransferase catalytic pocket to enable cofactor binding, completion of base flipping, and catalysis. Bound unmethylated DNA does not open the catalytic pocket and is instead ejected upon ATP binding, driving high fidelity. This unprecedented chaperone-like, enzyme-remodeling role of the SNF2 ATPase domain illuminates how energy is used to enable faithful epigenetic memory. | ||
| + | |||
| + | Structural insights into DNMT5-mediated ATP-dependent high-fidelity epigenome maintenance.,Wang J, Catania S, Wang C, de la Cruz MJ, Rao B, Madhani HD, Patel DJ Mol Cell. 2022 Feb 16. pii: S1097-2765(22)00104-6. doi:, 10.1016/j.molcel.2022.01.028. PMID:35202575<ref>PMID:35202575</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7r77" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Cryptococcus neoformans]] | ||
| + | [[Category: Cryptococcus neoformans var. grubii H99]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Patel DJ]] |
| + | [[Category: Wang J]] | ||
Current revision
Cryo-EM structure of DNMT5 binary complex with hemimethylated DNA
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