3EFY
Structure of the Cyclomodulin Cif from Pathogenic Escherichia coli
Summary for 3EFY
| Entry DOI | 10.2210/pdb3efy/pdb |
| Descriptor | Cif (Cell cycle inhibiting factor) (2 entities in total) |
| Functional Keywords | cif, cell cycle, bacteria, virulence factor, type iii secretion, e. coli, plasmid |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 44880.87 |
| Authors | Stebbins, C.E.,Hsu, Y. (deposition date: 2008-09-10, release date: 2008-10-28, Last modification date: 2024-02-21) |
| Primary citation | Hsu, Y.,Jubelin, G.,Taieb, F.,Nougayrede, J.P.,Oswald, E.,Stebbins, C.E. Structure of the cyclomodulin Cif from pathogenic Escherichia coli. J.Mol.Biol., 384:465-477, 2008 Cited by PubMed Abstract: Bacterial pathogens have evolved a sophisticated arsenal of virulence factors to modulate host cell biology. Enteropathogenic and enterohemorrhagic Escherichia coli (EPEC and EHEC) use a type III protein secretion system (T3SS) to inject microbial proteins into host cells. The T3SS effector cycle inhibiting factor (Cif) produced by EPEC and EHEC is able to block host eukaryotic cell-cycle progression. We present here a crystal structure of Cif, revealing it to be a divergent member of the superfamily of enzymes including cysteine proteases and acetyltransferases that share a common catalytic triad. Mutation of these conserved active site residues abolishes the ability of Cif to block cell-cycle progression. Finally, we demonstrate that irreversible cysteine protease inhibitors do not abolish the Cif cytopathic effect, suggesting that another enzymatic activity may underlie the biological activity of this virulence factor. PubMed: 18845161DOI: 10.1016/j.jmb.2008.09.051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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