9v4o

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Current revision (06:35, 26 November 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9v4o is ON HOLD until Paper Publication
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==Cryo-EM structure of A. thaliana MET1 with bound SAH==
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<StructureSection load='9v4o' size='340' side='right'caption='[[9v4o]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9v4o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9V4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9V4O FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.92&#8491;</td></tr>
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<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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9v4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9v4o OCA], [https://pdbe.org/9v4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9v4o RCSB], [https://www.ebi.ac.uk/pdbsum/9v4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9v4o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DNMT1_ARATH DNMT1_ARATH] Maintains chromatin CpG methylation that plays a role in genomic imprinting, regulation of embryogenesis and seed viability. Required for proper patterns of CG DNA methylation in dividing cells. Required for MEA promoter methylation in seeds.<ref>PMID:12456661</ref> <ref>PMID:12663548</ref> <ref>PMID:12669067</ref> <ref>PMID:14667411</ref> <ref>PMID:16531498</ref> <ref>PMID:17012404</ref> <ref>PMID:18820427</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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DNA methylation plays critical roles in eukaryotic gene silencing, genome defense, and the suppression of transposable elements. During DNA replication, DNA methylation is diluted and must therefore be restored through maintenance DNA methylation. In plants, in addition to symmetric CG methylation, non-CG methylation is also abundant, with the maintenance of each DNA methylation pattern employing different pathways. Here, we investigate the molecular basis of CG maintenance methylation by plant METHYLTRANSFERASE 1 (MET1), an ortholog of mammalian DNA Methyltransferase 1 (DNMT1). The cryogenic electron microscopy structure of full-length Arabidopsis (Arabidopsis thaliana) MET1 reveals a unique autoinhibitory mechanism that is distinct from that of DNMT1. The structure of the MET1 catalytic domain in complex with hemimethylated substrate DNA suggests specific recognition of hemimethylated CG DNA and reveals the catalytic mechanism. Overall, our study illuminates the molecular basis of MET1 autoinhibition and its preference for hemimethylated DNA substrates.
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Authors:
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Structural insights into plant DNA CG methylation maintenance by MET1.,Zhang Z, Li W, Liu Y, Chi C, Nan J, Wang C, Zhu Y, Zhao J, Xue Y, Li Y, Wang P, Zhai J, Du J Plant Cell. 2025 Oct 31;37(11):koaf244. doi: 10.1093/plcell/koaf244. PMID:41082561<ref>PMID:41082561</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9v4o" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arabidopsis thaliana]]
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[[Category: Large Structures]]
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[[Category: Du J]]
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[[Category: Li W]]
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[[Category: Liu Y]]
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[[Category: Zhang Z]]

Current revision

Cryo-EM structure of A. thaliana MET1 with bound SAH

PDB ID 9v4o

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