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

Authors :
Jantarit N
Tanaka H
Lin Y
Lee YH
Kurisu G
Source :
FEBS open bio [FEBS Open Bio] 2024 Oct; Vol. 14 (10), pp. 1731-1745. Date of Electronic Publication: 2024 Aug 09.
Publication Year :
2024

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.<br /> (© 2024 The Author(s). FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)

Details

Language :
English
ISSN :
2211-5463
Volume :
14
Issue :
10
Database :
MEDLINE
Journal :
FEBS open bio
Publication Type :
Academic Journal
Accession number :
39123319
Full Text :
https://doi.org/10.1002/2211-5463.13874