View source for 6vgt


==Solution NMR structure of enterococcal cytolysin L (CylLL") produced by Enterococcus faecalis==
<StructureSection load='6vgt' size='340' side='right'caption='[[6vgt]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6vgt]] 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=6VGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VGT FirstGlance]. <br>
</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>, <scene name='pdbligand=DHA:2-AMINO-ACRYLIC+ACID'>DHA</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=6vgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vgt OCA], [https://pdbe.org/6vgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vgt RCSB], [https://www.ebi.ac.uk/pdbsum/6vgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vgt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H7C7B0_ENTFA H7C7B0_ENTFA] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:34094481</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6vgt" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytolysin 3D structures|Cytolysin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Enterococcus faecalis]]
[[Category: Large Structures]]
[[Category: Bobeica SC]]
[[Category: Tang W]]
[[Category: Zhu L]]
[[Category: Van der Donk WA]]