8JC1

Crystal structure of Pectocin M1 from Pectobacterium carotovorum

8JC1 の概要

• エントリーDOI: 10.2210/pdb8jc1/pdb
• 分子名称: pectocin M1, FE2/S2 (INORGANIC) CLUSTER, SODIUM ION, ... (9 entities in total)
• 機能のキーワード: bactereocin, pectocin m1, colicin, ferredoxin-like protein, peptidoglycan, hydrolase
• 由来する生物種: Pectobacterium carotovorum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 119098.24

構造登録者

Jantarit, N.,Kurisu, G.,Tanaka, H. (登録日: 2023-05-10, 公開日: 2024-09-04, 最終更新日: 2024-10-16)

主引用文献

Jantarit, N.,Tanaka, H.,Lin, Y.,Lee, Y.H.,Kurisu, G.
Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system.
Febs Open Bio, 14:1731-1745, 2024

PubMed Abstract: Pectocin M1 (PM1), the bacteriocin from phytopathogenic Pectobacterium carotovorum which causes soft rot disease, has a unique ferredoxin domain that allows it to use FusA of the plant ferredoxin uptake system. To probe the structure-based mechanism of PM1 uptake, we determined the X-ray structure of full-length PM1, containing an N-terminal ferredoxin and C-terminal catalytic domain connected by helical linker, at 2.04 Å resolution. Based on published FusA structure and NMR data for PM1 ferredoxin domain titrated with FusA, we modeled docking of the ferredoxin domain with FusA. Combining the docking models with the X-ray structures of PM1 and FusA enables us to propose the mechanism by which PM1 undergoes dynamic domain rearrangement to translocate across the target cell outer membrane.

PubMed: 39123319
DOI: 10.1002/2211-5463.13874

実験手法

X-RAY DIFFRACTION (2.04 Å)