6sig: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6sig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sig OCA], [https://pdbe.org/6sig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sig RCSB], [https://www.ebi.ac.uk/pdbsum/6sig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sig 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=6sig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sig OCA], [https://pdbe.org/6sig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sig RCSB], [https://www.ebi.ac.uk/pdbsum/6sig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sig ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteriocins are a distinct family of antimicrobial proteins postulated to porate bacterial membranes. However, direct experimental evidence of pore formation by these proteins is lacking. Here we report a multi-mode poration mechanism induced by four-helix bacteriocins, epidermicin NI01 and aureocin A53. Using a combination of crystallography, spectroscopy, bioassays, and nanoscale imaging, we established that individual two-helix segments of epidermicin retain antibacterial activity but each of these segments adopts a particular poration mode. In the intact protein these segments act synergistically to balance out antibacterial and hemolytic activities. The study sets a precedent of multi-mode membrane disruption advancing the current understanding of structure-activity relationships in pore-forming proteins. | |||
Flowering Poration-A Synergistic Multi-Mode Antibacterial Mechanism by a Bacteriocin Fold.,Hammond K, Lewis H, Halliwell S, Desriac F, Nardone B, Ravi J, Hoogenboom BW, Upton M, Derrick JP, Ryadnov MG iScience. 2020 Aug 21;23(8):101423. doi: 10.1016/j.isci.2020.101423. Epub 2020, Jul 30. PMID:32795916<ref>PMID:32795916</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 6sig" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:41, 31 March 2021
Epidermicin antimicrobial protein from Staphylococcus epidermidisEpidermicin antimicrobial protein from Staphylococcus epidermidis
Structural highlights
Publication Abstract from PubMedBacteriocins are a distinct family of antimicrobial proteins postulated to porate bacterial membranes. However, direct experimental evidence of pore formation by these proteins is lacking. Here we report a multi-mode poration mechanism induced by four-helix bacteriocins, epidermicin NI01 and aureocin A53. Using a combination of crystallography, spectroscopy, bioassays, and nanoscale imaging, we established that individual two-helix segments of epidermicin retain antibacterial activity but each of these segments adopts a particular poration mode. In the intact protein these segments act synergistically to balance out antibacterial and hemolytic activities. The study sets a precedent of multi-mode membrane disruption advancing the current understanding of structure-activity relationships in pore-forming proteins. Flowering Poration-A Synergistic Multi-Mode Antibacterial Mechanism by a Bacteriocin Fold.,Hammond K, Lewis H, Halliwell S, Desriac F, Nardone B, Ravi J, Hoogenboom BW, Upton M, Derrick JP, Ryadnov MG iScience. 2020 Aug 21;23(8):101423. doi: 10.1016/j.isci.2020.101423. Epub 2020, Jul 30. PMID:32795916[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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