7xno
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Cryo-EM structure of the bacteriocin-receptor-immunity ternary complex from Lactobacillus sakei== |
| - | <StructureSection load='7xno' size='340' side='right'caption='[[7xno]]' scene=''> | + | <StructureSection load='7xno' size='340' side='right'caption='[[7xno]], [[Resolution|resolution]] 2.54Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7xno]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Latilactobacillus_sakei_L45 Latilactobacillus sakei L45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XNO FirstGlance]. <br> |
| - | </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=7xno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xno OCA], [https://pdbe.org/7xno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xno RCSB], [https://www.ebi.ac.uk/pdbsum/7xno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xno ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=7xno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xno OCA], [https://pdbe.org/7xno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xno RCSB], [https://www.ebi.ac.uk/pdbsum/7xno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xno ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/SAKA_LATSK SAKA_LATSK]] Bactericidal activity; inhibits closely related Lactobacilli, Listeria monocytogenes and ivanovvi, Enterococcus faecalis, Carnobacterium sp and Brocothrix thermosphacta. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pediocin-like bacteriocins, also designated class IIa bacteriocins, are ribosomally synthesized antimicrobial peptides targeting species closely related to the producers. They act on the cytoplasmic membrane of Gram-positive cells by dissipating the transmembrane electrical potential through pore formation with the mannose phosphotransferase system (man-PTS) as the target/receptor. Bacteriocin-producing strains also synthesize a cognate immunity protein that protects them against their own bacteriocins. Herein, we report the cryo-electron microscopy structure of the bacteriocin-receptor-immunity ternary complex from Lactobacillus sakei. The complex structure reveals that pediocin-like bacteriocins bind to the same position on the Core domain of man-PTS, while the C-terminal helical tails of bacteriocins delimit the opening range of the Core domain away from the Vmotif domain to facilitate transmembrane pore formation. Upon attack of bacteriocins from the extracellular side, man-PTS exposes its cytosolic side for recognition of the N-terminal four-helix bundle of the immunity protein. The C-terminal loop of the immunity protein then inserts into the pore and blocks leakage induced by bacteriocins. Elucidation of the toxicity and immunity mechanisms of pediocin-like bacteriocins could support the design of novel bacteriocins against antibiotic-resistant pathogenic bacteria. IMPORTANCE Pediocin-like bacteriocins, ribosomally synthesized antimicrobial peptides, are generally co-expressed with cognate immunity proteins to protect the bacteriocin-producing strain from its own bacteriocin. Bacteriocins are considered potential alternatives to conventional antibiotics in the context of the bacterial resistance crisis, but the immunity mechanism is unclear. This study uncovered the mechanisms of action and immunity of class IIa bacteriocins. | ||
| + | |||
| + | Structural Basis of the Immunity Mechanisms of Pediocin-like Bacteriocins.,Zhu L, Zeng J, Wang J Appl Environ Microbiol. 2022 Jul 12;88(13):e0048122. doi: 10.1128/aem.00481-22., Epub 2022 Jun 15. PMID:35703550<ref>PMID:35703550</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7xno" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Latilactobacillus sakei L45]] |
| + | [[Category: Wang JW]] | ||
Current revision
Cryo-EM structure of the bacteriocin-receptor-immunity ternary complex from Lactobacillus sakei
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