6sig

Epidermicin antimicrobial protein from Staphylococcus epidermidisEpidermicin antimicrobial protein from Staphylococcus epidermidis

Structural highlights 6sig is a 4 chain structure with sequence from Staphylococcus epidermidis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.58Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H9BG66_STAEP 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6sig, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image