6SIG

Epidermicin antimicrobial protein from Staphylococcus epidermidis

6SIG の概要

• エントリーDOI: 10.2210/pdb6sig/pdb
• 分子名称: Epidermicin locus structural protein, SULFATE ION (3 entities in total)
• 機能のキーワード: antibiotic, helical, structural protein
• 由来する生物種: Staphylococcus epidermidis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 24409.35

構造登録者

Derrick, J.P. (登録日: 2019-08-09, 公開日: 2020-08-26, 最終更新日: 2024-01-24)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.58 Å)