9EUW
Lymphostatin, conformation 2 (composite structure)
Summary for 9EUW
| Entry DOI | 10.2210/pdb9euw/pdb |
| Related | 9EUV |
| EMDB information | 19982 19983 19987 19988 |
| Descriptor | Efa1/LifA protein (1 entity in total) |
| Functional Keywords | bacterial virulence factor, glycosyltransferase, protease, toxin |
| Biological source | Escherichia coli O127:H6 str. E2348/69 |
| Total number of polymer chains | 1 |
| Total formula weight | 367234.06 |
| Authors | Griessmann, M.,Rasmussen, T.,Bottcher, B. (deposition date: 2024-03-28, release date: 2025-04-09, Last modification date: 2025-07-23) |
| Primary citation | Griessmann, M.,Rasmussen, T.,Flegler, V.J.,Kraft, C.,Schneider, R.,Hateley, M.,Spantzel, L.,Stevens, M.P.,Borsch, M.,Bottcher, B. Structure of lymphostatin, a large multi-functional virulence factor of pathogenic Escherichia coli. Nat Commun, 16:5389-5389, 2025 Cited by PubMed Abstract: Lymphostatin is a key virulence factor of enteropathogenic and enterohaemorrhagic Escherichia coli, playing roles in bacterial colonisation of the gut and in the inhibition of lymphocyte proliferation and proinflammatory responses. The protein's glycosyltransferase and cysteine protease motifs are required for activity against lymphocytes, but high-resolution structural information has proven elusive. Here, we describe the structure of lymphostatin from enteropathogenic E. coli O127:H6, determined by electron cryo-microscopy at different pH values. We observe three conformations of a highly complex molecule with two glycosyltransferase domains, one PaToxP-like protease domain, an ADP-ribosyltransferase domain, a vertex domain and a delivery domain. Long linkers hold these domains together and occlude the catalytic sites of the N-terminal glycosyltransferase and protease domains. Lymphostatin binds to bovine T-lymphocytes and HEK-293T cells, forming clusters at the plasma membrane that are internalized. With six distinct domains, lymphostatin can be regarded as a multitool of pathogenic Escherichia coli, enabling complex interactions with host cells. PubMed: 40562750DOI: 10.1038/s41467-025-60995-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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