6sig: Difference between revisions

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-'''Unreleased structure'''
-The entry 6sig is ON HOLD  until Paper Publication
+==Epidermicin antimicrobial protein from Staphylococcus epidermidis==
+<StructureSection load='6sig' size='340' side='right'caption='[[6sig]], [[Resolution|resolution]] 1.58&Aring;' 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]] 1.58&#8491;</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.
-Authors: Derrick, J.P.
+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>
-Description: Epidermicin antimicrobial protein from Staphylococcus epidermidis
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Derrick, J.P]]
+<div class="pdbe-citations 6sig" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Staphylococcus epidermidis]]
+[[Category: Derrick JP]]