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| | <StructureSection load='6azt' size='340' side='right'caption='[[6azt]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='6azt' size='340' side='right'caption='[[6azt]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6azt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_sunflower Common sunflower]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AZT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6azt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AZT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CE7:'>CE7</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CE7:(3S)-3-amino-4,4,4-trihydroxybutanamide'>CE7</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AEP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4232 Common sunflower])</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=6azt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6azt OCA], [https://pdbe.org/6azt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6azt RCSB], [https://www.ebi.ac.uk/pdbsum/6azt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6azt ProSAT]</span></td></tr> |
| - | <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=6azt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6azt OCA], [http://pdbe.org/6azt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6azt RCSB], [http://www.ebi.ac.uk/pdbsum/6azt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6azt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A251RPF5_HELAN A0A251RPF5_HELAN] |
| | <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: Common sunflower]] | + | [[Category: Helianthus annuus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bond, C S]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Plant protein]] | + | [[Category: Bond CS]] |
| Structural highlights
Function
A0A251RPF5_HELAN
Publication Abstract from PubMed
Constrained, cyclic peptides encoded by plant genes represent a new generation of drug leads. Evolution has repeatedly recruited the Cys-protease asparaginyl endopeptidase (AEP) to perform their head-to-tail ligation. These macrocyclization reactions use the substrates amino terminus instead of water to deacylate, so a peptide bond is formed. How solvent-exposed plant AEPs macrocyclize is poorly understood. Here we present the crystal structure of an active plant AEP from the common sunflower, Helianthus annuus. The active site contained electron density for a tetrahedral intermediate with partial occupancy that predicted a binding mode for peptide macrocyclization. By substituting catalytic residues we could alter the ratio of cyclic to acyclic products. Moreover, we showed AEPs from other species lacking cyclic peptides can perform macrocyclization under favorable pH conditions. This structural characterization of AEP presents a logical framework for engineering superior enzymes that generate macrocyclic peptide drug leads.
Structural basis of ribosomal peptide macrocyclization in plants.,Haywood J, Schmidberger JW, James AM, Nonis SG, Sukhoverkov KV, Elias M, Bond CS, Mylne JS Elife. 2018 Jan 31;7. pii: 32955. doi: 10.7554/eLife.32955. PMID:29384475[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Haywood J, Schmidberger JW, James AM, Nonis SG, Sukhoverkov KV, Elias M, Bond CS, Mylne JS. Structural basis of ribosomal peptide macrocyclization in plants. Elife. 2018 Jan 31;7. pii: 32955. doi: 10.7554/eLife.32955. PMID:29384475 doi:http://dx.doi.org/10.7554/eLife.32955
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