Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system

Jantarit, Nawee; Tanaka, Hideaki; Lin, Yuxi et al.

FEBS Open Bio, 2024, 14(10), 1731-1745

アクセス数:76件（2025-05-18 10:31 集計）

固定URL: https://hdl.handle.net/11094/98134

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タイトル
Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system
著者
著者名
Jantarit, Nawee
NRID
1000040346169 1000040346169
著者名
Tanaka, Hideaki
著者名
Lin, Yuxi
著者名
Lee, Young Ho
NRID
1000090294131 1000090294131
ORCID
0000-0002-5354-0807 0000-0002-5354-0807
researchmap permalink
read0051718 read0051718
Scopus Author ID
6701675123 6701675123
著者名
Kurisu, Genji
キーワード等
bacteriocin
ferredoxin
lipid-II-degrading enzyme
Pectobacterium
siderophore
X-ray crystallography
内容
Jantarit N., Tanaka H., Lin Y., et al. Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system. FEBS Open Bio, (2024); https://doi.org/10.1002/2211-5463.13874.
抄録
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.
出版者
John Wiley and Sons Inc
収録物名
FEBS Open Bio
巻(号)
14(10)
ページ
1731-1745
刊行年月
2024-08-09
言語
英語
ハンドルURL
https://hdl.handle.net/11094/98134
eISSN
22115463
関連情報 (isIdenticalTo)
DOI (出版社版)
https://doi.org/10.1002/2211-5463.13874
アクセス権
open access
権利情報
This article is licensed under a Creative Commons Attribution 4.0 International License.
出版タイプ
Version of Record
カテゴリ
学術雑誌論文 Journal Article