6PI5
The evolving story of AtzT, a periplasmic binding protein
Summary for 6PI5
| Entry DOI | 10.2210/pdb6pi5/pdb |
| Descriptor | Atrazine periplasmic binding protein, GUANINE, DIMETHYL SULFOXIDE, ... (4 entities in total) |
| Functional Keywords | sad phasing, periplasmic binding protein, evolution from purine binding to atrazine binding, transport protein |
| Biological source | Pseudomonas sp. (strain ADP) |
| Total number of polymer chains | 4 |
| Total formula weight | 153849.40 |
| Authors | Peat, T.S.,Newman, J.,Scott, C.,Esquirol, L.,Dennis, M.,Nebl, T. (deposition date: 2019-06-26, release date: 2019-11-13, Last modification date: 2023-10-11) |
| Primary citation | Dennis, M.L.,Esquirol, L.,Nebl, T.,Newman, J.,Scott, C.,Peat, T.S. The evolving story of AtzT, a periplasmic binding protein. Acta Crystallogr D Struct Biol, 75:995-1002, 2019 Cited by PubMed Abstract: Atrazine is an s-triazine-based herbicide that is used in many countries around the world in many millions of tons per year. A small number of organisms, such as Pseudomonas sp. strain ADP, have evolved to use this modified s-triazine as a food source, and the various genes required to metabolize atrazine can be found on a single plasmid. The atomic structures of seven of the eight proteins involved in the breakdown of atrazine by Pseudomonas sp. strain ADP have been determined by X-ray crystallography, but the structures of the proteins required by the cell to import atrazine for use as an energy source are still lacking. The structure of AtzT, a periplasmic binding protein that may be involved in the transport of a derivative of atrazine, 2-hydroxyatrazine, into the cell for mineralization, has now been determined. The structure was determined by SAD phasing using an ethylmercury phosphate derivative that diffracted X-rays to beyond 1.9 Å resolution. `Native' (guanine-bound) and 2-hydroxyatrazine-bound structures were also determined to high resolution (1.67 and 1.65 Å, respectively), showing that 2-hydroxyatrazine binds in a similar way to the purportedly native ligand. Structural similarities led to the belief that it may be possible to evolve AtzT from a purine-binding protein to a protein that can bind and detect atrazine in the environment. PubMed: 31692473DOI: 10.1107/S2059798319013883 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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