7AQS
Crystal structure of E. coli DPS in space group P1
Summary for 7AQS
| Entry DOI | 10.2210/pdb7aqs/pdb |
| Descriptor | DNA protection during starvation protein, FE (III) ION (3 entities in total) |
| Functional Keywords | dna protection during starvation protein, an impurity of colicin preparation, iron, dna binding protein |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 24 |
| Total formula weight | 455129.28 |
| Authors | Jakob, R.P.,Pipercevic, J.,Righetto, R.,Goldie, K.,Stahlberg, H.,Maier, T.,Hiller, S. (deposition date: 2020-10-22, release date: 2021-09-01, Last modification date: 2024-10-16) |
| Primary citation | Pipercevic, J.,Jakob, R.P.,Righetto, R.D.,Goldie, K.N.,Stahlberg, H.,Maier, T.,Hiller, S. Identification of a Dps contamination in Mitomycin-C-induced expression of Colicin Ia. Biochim Biophys Acta Biomembr, 1863:183607-183607, 2021 Cited by PubMed Abstract: Colicins are bacterial toxins targeting Gram-negative bacteria, including E. coli and related Enterobacteriaceae strains. Some colicins form ion-gated pores in the inner membrane of attacked bacteria that are lethal to their target. Colicin Ia was the first pore-forming E. coli toxin, for which a high-resolution structure of the monomeric full-length protein was determined. It is so far also the only colicin, for which a low-resolution structure of its membrane-inserted pore was reported by negative-stain electron microscopy. Resolving this structure at the atomic level would allow an understanding of the mechanism of toxin pore formation. Here, we report an observation that we made during an attempt to determine the Colicin Ia pore structure at atomic resolution. Colicin Ia was natively expressed by mitomycin-C induction under a native SOS promotor and purified following published protocols. The visual appearance in the electron microscope of negatively stained preparations and the lattice parameters of 2D crystals obtained from the material were highly similar to those reported earlier resulting from the same purification protocol. However, a higher-resolution structural analysis revealed that the protein is Dps (DNA-binding protein from starved cells), a dodecameric E. coli protein. This finding suggests that the previously reported low-resolution structure of a "Colicin Ia oligomeric pore" actually shows Dps. PubMed: 33775657DOI: 10.1016/j.bbamem.2021.183607 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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