View source for 7yi8


==Cryo-EM structure of SAH-bound MTA1-MTA9-p1-p2 complex==
<StructureSection load='7yi8' size='340' side='right'caption='[[7yi8]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yi8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila_SB210 Tetrahymena thermophila SB210]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YI8 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=7yi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yi8 OCA], [https://pdbe.org/7yi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yi8 RCSB], [https://www.ebi.ac.uk/pdbsum/7yi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yi8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I7M8B9_TETTS I7M8B9_TETTS] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N(6)-methyldeoxyadenine (6mA) has recently been reported as a prevalent DNA modification in eukaryotes. The Tetrahymena thermophila MTA1 complex consisting of four subunits, namely MTA1, MTA9, p1, and p2, is the first identified eukaryotic 6mA methyltransferase (MTase) complex. Unlike the prokaryotic 6mA MTases which have been biochemically and structurally characterized, the operation mode of the MTA1 complex remains largely elusive. Here, we report the cryogenic electron microscopy structures of the quaternary MTA1 complex in S-adenosyl methionine (SAM)-bound (2.6 A) and S-adenosyl homocysteine (SAH)-bound (2.8 A) states. Using an AI-empowered integrative approach based on AlphaFold prediction and chemical cross-linking mass spectrometry, we further modeled a near-complete structure of the quaternary complex. Coupled with biochemical characterization, we revealed that MTA1 serves as the catalytic core, MTA1, MTA9, and p1 likely accommodate the substrate DNA, and p2 may facilitate the stabilization of MTA1. These results together offer insights into the molecular mechanism underpinning methylation by the MTA1 complex and the potential diversification of MTases for N(6)-adenine methylation.

Structural insights into DNA N(6)-adenine methylation by the MTA1 complex.,Yan J, Liu F, Guan Z, Yan X, Jin X, Wang Q, Wang Z, Yan J, Zhang D, Liu Z, Wu S, Yin P Cell Discov. 2023 Jan 20;9(1):8. doi: 10.1038/s41421-022-00516-w. PMID:36658132<ref>PMID:36658132</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yi8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tetrahymena thermophila SB210]]
[[Category: Guan ZY]]
[[Category: Hou MJ]]
[[Category: Liu FQ]]
[[Category: Yan JJ]]
[[Category: Yan XH]]
[[Category: Yin P]]