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6sig
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6sig is ON HOLD Authors: Derrick, J.P. Description: Epidermicin antimicrobial protein from Staphylococcus epidermidis [[Category: Unreleased Struct...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Epidermicin antimicrobial protein from Staphylococcus epidermidis== | |
| + | <StructureSection load='6sig' size='340' side='right'caption='[[6sig]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6sig]] is a 4 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=6SIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SIG FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</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=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> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/H9BG66_STAEP H9BG66_STAEP] | ||
| + | <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> |
| - | [[Category: Derrick | + | <div class="pdbe-citations 6sig" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Staphylococcus epidermidis]] | ||
| + | [[Category: Derrick JP]] | ||
Current revision
Epidermicin antimicrobial protein from Staphylococcus epidermidis
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