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| | ==Solution NMR structure of enterococcal cytolysin S (CylLS") produced by Enterococcus faecalis== | | ==Solution NMR structure of enterococcal cytolysin S (CylLS") produced by Enterococcus faecalis== |
| - | <StructureSection load='6ve9' size='340' side='right'caption='[[6ve9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6ve9' size='340' side='right'caption='[[6ve9]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ve9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VE9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ve9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VE9 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DBU:(2Z)-2-AMINOBUT-2-ENOIC+ACID'>DBU</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DBU:(2Z)-2-AMINOBUT-2-ENOIC+ACID'>DBU</scene></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=6ve9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ve9 OCA], [https://pdbe.org/6ve9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ve9 RCSB], [https://www.ebi.ac.uk/pdbsum/6ve9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ve9 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=6ve9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ve9 OCA], [https://pdbe.org/6ve9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ve9 RCSB], [https://www.ebi.ac.uk/pdbsum/6ve9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ve9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/H7C7B5_ENTFA H7C7B5_ENTFA] |
| | <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: Enterococcus proteiformis thiercelin and jouhaud 1903]] | + | [[Category: Enterococcus faecalis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bobeica, S C]] | + | [[Category: Bobeica SC]] |
| - | [[Category: Donk, W A.van der]]
| + | [[Category: Tang W]] |
| - | [[Category: Tang, W]] | + | [[Category: Zhu L]] |
| - | [[Category: Zhu, L]] | + | [[Category: Van der Donk WA]] |
| - | [[Category: Cyclic peptide]] | + | |
| - | [[Category: Cytolysin]]
| + | |
| - | [[Category: Lanthipeptide]]
| + | |
| - | [[Category: Posttranslational modification]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
H7C7B5_ENTFA
Publication Abstract from PubMed
Lanthipeptides are characterized by thioether crosslinks formed by post-translational modifications. The cyclization process that favors a single ring pattern over many other possible ring patterns has been the topic of much speculation. Recent studies suggest that for some systems the cyclization pattern and stereochemistry is determined not by the enzyme, but by the sequence of the precursor peptide. However, the factors that govern the outcome of the cyclization process are not understood. This study presents the three-dimensional structures of seven lanthipeptides determined by nuclear magnetic resonance spectroscopy, including five prochlorosins and the two peptides that make up cytolysin, a virulence factor produced by Enterococcus faecalis that is directly linked to human disease. These peptides were chosen because their substrate sequence determines either the ring pattern (prochlorosins) or the stereochemistry of cyclization (cytolysins). We present the structures of prochlorosins 1.1, 2.1, 2.8, 2.10 and 2.11, the first three-dimensional structures of prochlorosins. Our findings provide insights into the molecular determinants of cyclization as well as why some prochlorosins may be better starting points for library generation than others. The structures of the large and small subunits of the enterococcal cytolysin show that these peptides have long helical stretches, a rare observation for lanthipeptides characterized to date. These helices may explain their pore forming activity and suggest that the small subunit may recognize a molecular target followed by recruitment of the large subunit to span the membrane.
Structural determinants of macrocyclization in substrate-controlled lanthipeptide biosynthetic pathways.,Bobeica SC, Zhu L, Acedo JZ, Tang W, van der Donk WA Chem Sci. 2020 Jun 25;11(47):12854-12870. doi: 10.1039/d0sc01651a. PMID:34094481[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bobeica SC, Zhu L, Acedo JZ, Tang W, van der Donk WA. Structural determinants of macrocyclization in substrate-controlled lanthipeptide biosynthetic pathways. Chem Sci. 2020 Jun 25;11(47):12854-12870. doi: 10.1039/d0sc01651a. PMID:34094481 doi:http://dx.doi.org/10.1039/d0sc01651a
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