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4qep

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==crystal structure of KRYPTONITE in complex with mCHG DNA and SAH==
==crystal structure of KRYPTONITE in complex with mCHG DNA and SAH==
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<StructureSection load='4qep' size='340' side='right' caption='[[4qep]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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<StructureSection load='4qep' size='340' side='right'caption='[[4qep]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QEP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4qep]] is a 3 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=4QEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QEP FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene></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=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene>, <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qen|4qen]], [[4qeo|4qeo]]</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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [https://pdbe.org/4qep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [https://www.ebi.ac.uk/pdbsum/4qep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qep ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [http://pdbe.org/4qep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [http://www.ebi.ac.uk/pdbsum/4qep PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qep ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SUVH4_ARATH SUVH4_ARATH]] Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. The silencing mechanism via DNA CpNpG methylation requires the targeting of chromomethylase CMT3 to methylated histones, probably through an interaction with an HP1-like adapter. By its function, KYP is directly required for the maintenance of the DNA CpNpG and asymmetric methylation. Involved in the silencing of transposable elements.<ref>PMID:11898023</ref> <ref>PMID:15457214</ref> <ref>PMID:15598823</ref> <ref>PMID:16277745</ref> <ref>PMID:16287862</ref>
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[https://www.uniprot.org/uniprot/SUVH4_ARATH SUVH4_ARATH] Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. The silencing mechanism via DNA CpNpG methylation requires the targeting of chromomethylase CMT3 to methylated histones, probably through an interaction with an HP1-like adapter. By its function, KYP is directly required for the maintenance of the DNA CpNpG and asymmetric methylation. Involved in the silencing of transposable elements.<ref>PMID:11898023</ref> <ref>PMID:15457214</ref> <ref>PMID:15598823</ref> <ref>PMID:16277745</ref> <ref>PMID:16287862</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4qep" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4qep" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone-lysine N-methyltransferase]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Du, J]]
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[[Category: Large Structures]]
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[[Category: Li, S]]
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[[Category: Du J]]
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[[Category: Patel, D J]]
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[[Category: Li S]]
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[[Category: Histone methylation]]
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[[Category: Patel DJ]]
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[[Category: Methylated dna]]
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[[Category: Methylation]]
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[[Category: Set]]
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[[Category: Sra]]
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[[Category: Transcription-dna complex]]
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Current revision

crystal structure of KRYPTONITE in complex with mCHG DNA and SAH

PDB ID 4qep

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