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| | ==Solution NMR of Prochlorosin 1.1 produced by Prochlorococcus MIT 9313== | | ==Solution NMR of Prochlorosin 1.1 produced by Prochlorococcus MIT 9313== |
| - | <StructureSection load='6vhj' size='340' side='right'caption='[[6vhj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6vhj' size='340' side='right'caption='[[6vhj]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6vhj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Promm Promm]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VHJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vhj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Prochlorococcus_marinus_str._MIT_9313 Prochlorococcus marinus str. MIT 9313]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VHJ FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</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=6vhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vhj OCA], [https://pdbe.org/6vhj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vhj RCSB], [https://www.ebi.ac.uk/pdbsum/6vhj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vhj 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=6vhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vhj OCA], [https://pdbe.org/6vhj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vhj RCSB], [https://www.ebi.ac.uk/pdbsum/6vhj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vhj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LAN11_PROMM LAN11_PROMM] Lanthionine-containing peptide (lantipeptide) with unknown function (Probable). Does not show antibiotic activity against Lactococcus lactis 117 and Bacillus subtilis 6633 bacteria (PubMed:20479271). Organisms that produce this peptide live in oligotrophic environments at very dilute concentrations, suggesting this peptide is not secreted to influence other bacteria (Probable).<ref>PMID:20479271</ref> <ref>PMID:20479271</ref> <ref>PMID:22574919</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Promm]] | + | [[Category: Prochlorococcus marinus str. MIT 9313]] |
| - | [[Category: Bobeica, S C]] | + | [[Category: Bobeica SC]] |
| - | [[Category: Donk, W A.van der]]
| + | [[Category: Tang W]] |
| - | [[Category: Tang, W]] | + | [[Category: Van der Donk WA]] |
| - | [[Category: Cyclic peptide]] | + | |
| - | [[Category: Lanthipeptide]]
| + | |
| - | [[Category: Posttranslational modification]]
| + | |
| - | [[Category: Ripp]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
LAN11_PROMM Lanthionine-containing peptide (lantipeptide) with unknown function (Probable). Does not show antibiotic activity against Lactococcus lactis 117 and Bacillus subtilis 6633 bacteria (PubMed:20479271). Organisms that produce this peptide live in oligotrophic environments at very dilute concentrations, suggesting this peptide is not secreted to influence other bacteria (Probable).[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li B, Sher D, Kelly L, Shi Y, Huang K, Knerr PJ, Joewono I, Rusch D, Chisholm SW, van der Donk WA. Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobacteria. Proc Natl Acad Sci U S A. 2010 Jun 8;107(23):10430-5. doi:, 10.1073/pnas.0913677107. Epub 2010 May 17. PMID:20479271 doi:http://dx.doi.org/10.1073/pnas.0913677107
- ↑ Li B, Sher D, Kelly L, Shi Y, Huang K, Knerr PJ, Joewono I, Rusch D, Chisholm SW, van der Donk WA. Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobacteria. Proc Natl Acad Sci U S A. 2010 Jun 8;107(23):10430-5. doi:, 10.1073/pnas.0913677107. Epub 2010 May 17. PMID:20479271 doi:http://dx.doi.org/10.1073/pnas.0913677107
- ↑ Tang W, van der Donk WA. Structural characterization of four prochlorosins: a novel class of lantipeptides produced by planktonic marine cyanobacteria. Biochemistry. 2012 May 29;51(21):4271-9. doi: 10.1021/bi300255s. Epub 2012 May, 17. PMID:22574919 doi:http://dx.doi.org/10.1021/bi300255s
- ↑ 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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