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6mjf

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Current revision (14:43, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6mjf' size='340' side='right'caption='[[6mjf]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6mjf' size='340' side='right'caption='[[6mjf]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6mjf]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Dendrothele_bispora_cbs_962.96 Dendrothele bispora cbs 962.96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MJF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6mjf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendrothele_bispora_CBS_962.96 Dendrothele bispora CBS 962.96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MJF 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]] 2.198&#8491;</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=6mjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mjf OCA], [http://pdbe.org/6mjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mjf RCSB], [http://www.ebi.ac.uk/pdbsum/6mjf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mjf ProSAT]</span></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></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=6mjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mjf OCA], [https://pdbe.org/6mjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mjf RCSB], [https://www.ebi.ac.uk/pdbsum/6mjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mjf ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A452CSY8_DENBC A0A452CSY8_DENBC]
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N-methylation of nucleic acids, proteins, and peptides is a chemical modification with significant impact on biological regulation. Despite the simplicity of the structural change, N-methylation can influence diverse functions including epigenetics, protein complex formation, and microtubule stability. While there are limited examples of N-methylation of the alpha-amino group of bacterial and eukaryotic proteins, there are no examples of catalysts that carry out post-translation methylation of backbone amides in proteins or peptides. Recent studies have identified enzymes that catalyze backbone N-methylation on a peptide substrate, a reaction with little biochemical precedent, in a family of ribosomally synthesized natural products produced in basidiomycetes. Here, we describe the crystal structures of Dendrothele bispora dbOphMA, a methyltransferase that catalyzes multiple N-methylations on the peptide backbone. We further carry out biochemical studies of this catalyst to determine the molecular details that promote this unusual chemical transformation. The structural and biochemical framework described here could facilitate biotechnological applications of catalysts for the rapid production of backbone N-methylated peptides.
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Molecular Basis for Autocatalytic Backbone N-Methylation in RiPP Natural Product Biosynthesis.,Ongpipattanakul C, Nair SK ACS Chem Biol. 2018 Sep 25. doi: 10.1021/acschembio.8b00668. PMID:30204409<ref>PMID:30204409</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6mjf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dendrothele bispora cbs 962 96]]
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[[Category: Dendrothele bispora CBS 962 96]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Nair, S K]]
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[[Category: Nair SK]]
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[[Category: Ongpipatanakul, C]]
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[[Category: Ongpipatanakul C]]
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[[Category: Biosynthetic protein]]
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[[Category: Borosin]]
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[[Category: Methyltransferase]]
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Current revision

Catalytic Domain of dbOphMA

PDB ID 6mjf

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