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| | <StructureSection load='5v1v' size='340' side='right'caption='[[5v1v]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='5v1v' size='340' side='right'caption='[[5v1v]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5v1v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet1 Thet1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V1V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5v1v]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobaculum_terrenum_ATCC_BAA-798 Thermobaculum terrenum ATCC BAA-798]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V1V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v1u|5v1u]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tter_2832 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=525904 THET1])</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=5v1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1v OCA], [https://pdbe.org/5v1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v1v RCSB], [https://www.ebi.ac.uk/pdbsum/5v1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1v 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=5v1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1v OCA], [http://pdbe.org/5v1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v1v RCSB], [http://www.ebi.ac.uk/pdbsum/5v1v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/D1CIZ5_THET1 D1CIZ5_THET1] |
| - | Enzymes that generate ribosomally synthesized and posttranslationally modified peptide (RiPP) natural products have garnered significant interest, given their ability to produce large libraries of chemically diverse scaffolds. Such RiPP biosynthetic enzymes are predicted to bind their corresponding peptide substrates through sequence-specific recognition of the leader sequence, which is removed after the installation of posttranslational modifications on the core sequence. The conservation of the leader sequence within a given RiPP class, in otherwise disparate precursor peptides, further supports the notion that strict sequence specificity is necessary for leader peptide engagement. Here, we demonstrate that leader binding by a biosynthetic enzyme in the lasso peptide class of RiPPs is directed by a minimal number of hydrophobic interactions. Biochemical and structural data illustrate how a single leader-binding domain can engage sequence-divergent leader peptides using a conserved motif that facilitates hydrophobic packing. The presence of this simple motif in noncognate peptides results in low micromolar affinity binding by binding domains from several different lasso biosynthetic systems. We also demonstrate that these observations likely extend to other RiPP biosynthetic classes. The portability of the binding motif opens avenues for the engineering of semisynthetic hybrid RiPP products.
| + | |
| - | | + | |
| - | Steric complementarity directs sequence promiscuous leader binding in RiPP biosynthesis.,Chekan JR, Ongpipattanakul C, Nair SK Proc Natl Acad Sci U S A. 2019 Nov 26;116(48):24049-24055. doi:, 10.1073/pnas.1908364116. Epub 2019 Nov 12. PMID:31719203<ref>PMID:31719203</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5v1v" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet1]] | + | [[Category: Thermobaculum terrenum ATCC BAA-798]] |
| - | [[Category: Chekan, J R]] | + | [[Category: Chekan JR]] |
| - | [[Category: Nair, S K]] | + | [[Category: Nair SK]] |
| - | [[Category: Lasso peptide]]
| + | |
| - | [[Category: Peptide binding]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Ripp]]
| + | |
