View source for 7ydw


==Crystal structure of the MPND-DNA complex==
<StructureSection load='7ydw' size='340' side='right'caption='[[7ydw]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ydw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=7YDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YDW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.47&#8491;</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=7ydw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ydw OCA], [https://pdbe.org/7ydw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ydw RCSB], [https://www.ebi.ac.uk/pdbsum/7ydw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ydw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MPND_MOUSE MPND_MOUSE] Probable protease (By similarity). Acts as a sensor of N(6)-methyladenosine methylation on DNA (m6A): recognizes and binds m6A DNA, leading to its degradation (By similarity).[UniProtKB:Q5VVJ2][UniProtKB:Q8N594]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Adenine N(6) methylation in DNA (6mA) is a well-known epigenetic modification in bacteria, phages, and eukaryotes. Recent research has identified the Mpr1/Pad1 N-terminal (MPN) domain-containing protein (MPND) as a sensor protein that may recognize DNA 6mA modification in eukaryotes. However, the structural details of MPND and the molecular mechanism of their interaction remain unknown. Herein, we report the first crystal structures of the apo-MPND and MPND-DNA complex at resolutions of 2.06 A and 2.47 A, respectively. In solution, the assemblies of both apo-MPND and MPND-DNA are dynamic. In addition, MPND was found to possess the ability to bind directly to histones, no matter the N-terminal restriction enzyme-adenine methylase-associated domain or the C-terminal MPN domain. Moreover, the DNA and the two acidic regions of MPND synergistically enhance the interaction between MPND and histones. Therefore, our findings provide the first structural information regarding the MPND-DNA complex and also provide evidence of MPND-nucleosome interactions, thereby laying the foundation for further studies on gene control and transcriptional regulation.

Structures of MPND Reveal the Molecular Recognition of Nucleosomes.,Yang M, Li X, Tian Z, Ma L, Ma J, Liu Y, Shang G, Liang A, Wu W, Chen Z Int J Mol Sci. 2023 Feb 8;24(4):3368. doi: 10.3390/ijms24043368. PMID:36834777<ref>PMID:36834777</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ydw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Synthetic construct]]
[[Category: Chen Z]]
[[Category: Yang M]]