6sif
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Epidermicin antimicrobial protein from Staphylococcus epidermidis== | |
| + | <StructureSection load='6sif' size='340' side='right'caption='[[6sif]], [[Resolution|resolution]] 1.69Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6sif]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SIF FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6sif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sif OCA], [https://pdbe.org/6sif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sif RCSB], [https://www.ebi.ac.uk/pdbsum/6sif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sif ProSAT]</span></td></tr> | ||
| + | </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> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6sif" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Staphylococcus epidermidis]] | ||
| + | [[Category: Derrick, J P]] | ||
| + | [[Category: Antibiotic]] | ||
| + | [[Category: Helical]] | ||
| + | [[Category: Structural protein]] | ||
Current revision
Epidermicin antimicrobial protein from Staphylococcus epidermidis
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