9vu6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of unmethylated DNA-bound Tetrahymena DNA methyltransferase complex MTA1c (MTA9-B)== | |
| + | <StructureSection load='9vu6' size='340' side='right'caption='[[9vu6]], [[Resolution|resolution]] 3.29Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9vu6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila_SB210 Tetrahymena thermophila SB210] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VU6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.29Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=9vu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vu6 OCA], [https://pdbe.org/9vu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vu6 RCSB], [https://www.ebi.ac.uk/pdbsum/9vu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vu6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q22GC0_TETTS Q22GC0_TETTS] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In eukaryotes, DNA N(6)-methyladenine (6mA) modification plays important roles in various cellular functions, such as chromatin dynamics, gene expression regulation, and DNA damage response. It remains largely unknown how eukaryotic DNA 6mA methyltransferases (MTases) recognize their substrates. Here, we reported the structures of DNA-bound eukaryotic 6mA MTase complexes. The MTA1 complex (MTA1c) in ciliates is composed of MTA1, MTA9 (or MTA9-B), p1 and p2 subunits. Cryo-electron microscopy structures of MTA1c-DNA complexes reveal that DNA lies on the surface of the MTA1-MTA9/9-B dimer and is clamped by the p1 N-terminal region. The target deoxyadenosine is flipped out of the DNA duplex and approaches the catalytic center. Unmethylated and hemi-methylated DNA substrates bind MTA1c with differential conformational dynamics. Our structural and biochemical studies shed light on the activation and substrate recognition of MTA1c and provide a framework for understanding the molecular mechanism of DNA 6mA modification in eukaryotes. | ||
| - | + | Mechanism for the substrate recognition by a eukaryotic DNA N(6)-adenine methyltransferase complex.,Xu Q, Xie Y, Shi Z Nat Commun. 2025 Sep 30;16(1):8690. doi: 10.1038/s41467-025-63738-y. PMID:41027852<ref>PMID:41027852</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9vu6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Tetrahymena thermophila SB210]] | ||
| + | [[Category: Shi ZB]] | ||
| + | [[Category: Xu Q]] | ||
Current revision
Cryo-EM structure of unmethylated DNA-bound Tetrahymena DNA methyltransferase complex MTA1c (MTA9-B)
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