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Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system.
- 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.)
- Subjects :
- Crystallography, X-Ray
Bacteriocins chemistry
Bacteriocins metabolism
Pectobacterium carotovorum metabolism
Pectobacterium carotovorum chemistry
Protein Conformation
Bacterial Proteins chemistry
Bacterial Proteins metabolism
Models, Molecular
Molecular Docking Simulation
Ferredoxins metabolism
Ferredoxins chemistry
Subjects
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