6SIF

Epidermicin antimicrobial protein from Staphylococcus epidermidis

Summary for 6SIF

• Entry DOI: 10.2210/pdb6sif/pdb
• Descriptor: Epidermicin locus structural protein, SULFATE ION (3 entities in total)
• Functional Keywords: antibiotic, helical, structural protein
• Biological source: Staphylococcus epidermidis
• Total number of polymer chains: 8
• Total formula weight: 49202.94

Authors

Derrick, J.P. (deposition date: 2019-08-09, release date: 2020-08-26, Last modification date: 2024-05-15)

Primary citation

Hammond, K.,Lewis, H.,Halliwell, S.,Desriac, F.,Nardone, B.,Ravi, J.,Hoogenboom, B.W.,Upton, M.,Derrick, J.P.,Ryadnov, M.G.
Flowering Poration-A Synergistic Multi-Mode Antibacterial Mechanism by a Bacteriocin Fold.
Iscience, 23:101423-101423, 2020

PubMed Abstract: 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.

PubMed: 32795916
DOI: 10.1016/j.isci.2020.101423

Experimental method

X-RAY DIFFRACTION (1.69 Å)