8JC1
Crystal structure of Pectocin M1 from Pectobacterium carotovorum
Summary for 8JC1
| Entry DOI | 10.2210/pdb8jc1/pdb |
| Descriptor | pectocin M1, FE2/S2 (INORGANIC) CLUSTER, SODIUM ION, ... (9 entities in total) |
| Functional Keywords | bactereocin, pectocin m1, colicin, ferredoxin-like protein, peptidoglycan, hydrolase |
| Biological source | Pectobacterium carotovorum |
| Total number of polymer chains | 4 |
| Total formula weight | 119098.24 |
| Authors | Jantarit, N.,Kurisu, G.,Tanaka, H. (deposition date: 2023-05-10, release date: 2024-09-04, Last modification date: 2024-10-16) |
| Primary citation | 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 Cited by 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: 39123319DOI: 10.1002/2211-5463.13874 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.04 Å) |
Structure validation
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