4Q8R
Crystal structure of a Phosphate Binding Protein (PBP-1) from Clostridium perfringens
Summary for 4Q8R
| Entry DOI | 10.2210/pdb4q8r/pdb |
| Related | 4GD5 |
| Descriptor | Phosphate ABC transporter, phosphate-binding protein, PHOSPHATE ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | periplasmic high affinity phosphate binding protein, transport protein |
| Biological source | Clostridium perfringens |
| Total number of polymer chains | 1 |
| Total formula weight | 27635.08 |
| Authors | Gonzalez, D.,Richez, M.,Bergonzi, C.,Chabriere, E.,Elias, M. (deposition date: 2014-04-28, release date: 2014-11-05, Last modification date: 2023-09-20) |
| Primary citation | Gonzalez, D.,Richez, M.,Bergonzi, C.,Chabriere, E.,Elias, M. Crystal structure of the phosphate-binding protein (PBP-1) of an ABC-type phosphate transporter from Clostridium perfringens. Sci Rep, 4:6636-6636, 2014 Cited by PubMed Abstract: Phosphate limitation is an important environmental stress that affects the metabolism of various organisms and, in particular, can trigger the virulence of numerous bacterial pathogens. Clostridium perfringens, a human pathogen, is one of the most common causes of enteritis necroticans, gas gangrene and food poisoning. Here, we focused on the high affinity phosphate-binding protein (PBP-1) of an ABC-type transporter, responsible for cellular phosphate uptake. We report the crystal structure (1.65 Å resolution) of the protein in complex with phosphate. Interestingly, PBP-1 does not form the short, low-barrier hydrogen bond with phosphate that is typical of previously characterized phosphate-binding proteins, but rather a canonical hydrogen bond. In its unique binding configuration, PBP-1 forms an unusually high number of hydrogen bonds (14) with the phosphate anion. Discrimination experiments reveal that PBP-1 is the least selective PBP characterised so far and is able to discriminate phosphate from its close competing anion, arsenate, by ~150-fold. PubMed: 25338617DOI: 10.1038/srep06636 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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