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| | <StructureSection load='6qzz' size='340' side='right'caption='[[6qzz]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='6qzz' size='340' side='right'caption='[[6qzz]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qzz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Jack_o'lantern Jack o'lantern]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QZZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QZZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qzz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Omphalotus_olearius Omphalotus olearius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QZZ FirstGlance]. <br> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=EME:N-METHYL-L-GLUTAMIC+ACID'>EME</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EME:N-METHYL-L-GLUTAMIC+ACID'>EME</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6qzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qzz OCA], [http://pdbe.org/6qzz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qzz RCSB], [http://www.ebi.ac.uk/pdbsum/6qzz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qzz ProSAT]</span></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=6qzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qzz OCA], [https://pdbe.org/6qzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qzz RCSB], [https://www.ebi.ac.uk/pdbsum/6qzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qzz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A2R2JFI5_OMPOL A0A2R2JFI5_OMPOL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Jack o'lantern]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Naismith, J H]] | + | [[Category: Omphalotus olearius]] |
| - | [[Category: Song, H]] | + | [[Category: Naismith JH]] |
| - | [[Category: Peptide bond n-methyltransferase]] | + | [[Category: Song H]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A0A2R2JFI5_OMPOL
Publication Abstract from PubMed
The methylation of amide nitrogen atoms can improve the stability, oral availability, and cell permeability of peptide therapeutics. Chemical N-methylation of peptides is challenging. Omphalotin A is a ribosomally synthesized, macrocylic dodecapeptide with nine backbone N-methylations. The fungal natural product is derived from the precursor protein, OphMA, harboring both the core peptide and a SAM-dependent peptide alpha-N-methyltransferase domain. OphMA forms a homodimer and its alpha-N-methyltransferase domain installs the methyl groups in trans on the hydrophobic core dodecapeptide and some additional C-terminal residues of the protomers. These post-translational backbone N-methylations occur in a processive manner from the N- to the C-terminus of the peptide substrate. We demonstrate that OphMA can methylate polar, aromatic, and charged residues when these are introduced into the core peptide. Some of these amino acids alter the efficiency and pattern of methylation. Proline, depending on its sequence context, can act as a tunable stop signal. Crystal structures of OphMA variants have allowed rationalization of these observations. Our results hint at the potential to control this fungal alpha-N-methyltransferase for biotechnological applications.
Substrate Plasticity of a Fungal Peptide alpha-N-Methyltransferase.,Song H, Fahrig-Kamarauskaite JR, Matabaro E, Kaspar H, Shirran SL, Zach C, Pace A, Stefanov BA, Naismith JH, Kunzler M ACS Chem Biol. 2020 Jun 19. doi: 10.1021/acschembio.0c00237. PMID:32491837[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Song H, Fahrig-Kamarauskaite JR, Matabaro E, Kaspar H, Shirran SL, Zach C, Pace A, Stefanov BA, Naismith JH, Kunzler M. Substrate Plasticity of a Fungal Peptide alpha-N-Methyltransferase. ACS Chem Biol. 2020 Jun 19. doi: 10.1021/acschembio.0c00237. PMID:32491837 doi:http://dx.doi.org/10.1021/acschembio.0c00237
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