6h1e

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Current revision (08:37, 11 December 2025) (edit) (undo)
 
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<StructureSection load='6h1e' size='340' side='right'caption='[[6h1e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6h1e' size='340' side='right'caption='[[6h1e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6h1e]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H1E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6h1e]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H1E 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></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]] 1.9&#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=MLZ:N-METHYL-LYSINE'>MLZ</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=MLZ:N-METHYL-LYSINE'>MLZ</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=6h1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h1e OCA], [http://pdbe.org/6h1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h1e RCSB], [http://www.ebi.ac.uk/pdbsum/6h1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h1e ProSAT]</span></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=6h1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h1e OCA], [https://pdbe.org/6h1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h1e RCSB], [https://www.ebi.ac.uk/pdbsum/6h1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h1e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/N6MT1_HUMAN N6MT1_HUMAN]] Methyltransferase that can methylate both proteins and DNA, and to a lower extent, arsenic (PubMed:18539146, PubMed:21193388, PubMed:30017583). Catalytic subunit of a heterodimer with TRMT112, which catalyzes N5-methylation of Glu residue of proteins with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif (PubMed:18539146) (By similarity). Methylates ETF1 on 'Gln-185'; ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated (PubMed:18539146, PubMed:20606008). Also acts as a N(6)-adenine-specific DNA methyltransferase by mediating methylation of DNA on the 6th position of adenine (N(6)-methyladenosine) (PubMed:30017583). N(6)-methyladenosine (m6A) DNA is significantly enriched in exonic regions and is associated with gene transcriptional activation (PubMed:30017583). May also play a role in the modulation of arsenic-induced toxicity by mediating the conversion of monomethylarsonous acid (3+) into the less toxic dimethylarsonic acid (PubMed:21193388, PubMed:25997655). It however only plays a limited role in arsenic metabolism compared with AS3MT (PubMed:25997655).[UniProtKB:Q6SKR2]<ref>PMID:18539146</ref> <ref>PMID:20606008</ref> <ref>PMID:21193388</ref> <ref>PMID:25997655</ref> <ref>PMID:30017583</ref> [[http://www.uniprot.org/uniprot/TR112_HUMAN TR112_HUMAN]] Acts as an activator of both rRNA/tRNA and protein methyltransferases (PubMed:25851604). Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA (PubMed:25851604). The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor (PubMed:18539146). The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species (PubMed:20308323). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production (PubMed:25851604).<ref>PMID:18539146</ref> <ref>PMID:20308323</ref> <ref>PMID:25851604</ref>
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[https://www.uniprot.org/uniprot/HEMK2_HUMAN HEMK2_HUMAN] Methyltransferase that can methylate both proteins and DNA, and to a lower extent, arsenic (PubMed:18539146, PubMed:21193388, PubMed:30017583). Catalytic subunit of a heterodimer with TRMT112, which catalyzes N5-methylation of Glu residue of proteins with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif (PubMed:18539146) (By similarity). Methylates ETF1 on 'Gln-185'; ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated (PubMed:18539146, PubMed:20606008). Also acts as a N(6)-adenine-specific DNA methyltransferase by mediating methylation of DNA on the 6th position of adenine (N(6)-methyladenosine) (PubMed:30017583). N(6)-methyladenosine (m6A) DNA is significantly enriched in exonic regions and is associated with gene transcriptional activation (PubMed:30017583). May also play a role in the modulation of arsenic-induced toxicity by mediating the conversion of monomethylarsonous acid (3+) into the less toxic dimethylarsonic acid (PubMed:21193388, PubMed:25997655). It however only plays a limited role in arsenic metabolism compared with AS3MT (PubMed:25997655).[UniProtKB:Q6SKR2]<ref>PMID:18539146</ref> <ref>PMID:20606008</ref> <ref>PMID:21193388</ref> <ref>PMID:25997655</ref> <ref>PMID:30017583</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 6h1e" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6h1e" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Einsle, O]]
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[[Category: Einsle O]]
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[[Category: Hermann, B]]
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[[Category: Hermann B]]
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[[Category: Metzger, E]]
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[[Category: Metzger E]]
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[[Category: Peng, L]]
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[[Category: Peng L]]
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[[Category: Schuele, R]]
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[[Category: Schuele R]]
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[[Category: Wang, S]]
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[[Category: Wang S]]
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[[Category: Complex]]
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[[Category: Gene regulation]]
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[[Category: Histone methylation]]
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[[Category: Protein methyltransferase]]
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[[Category: Sah]]
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Current revision

Crystal structure of C21orf127-TRMT112 in complex with SAH and H4 peptide

PDB ID 6h1e

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