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Sci Rep. 2014 Oct 16;4:6636. doi: 10.1038/srep06636.

Crystal structure of the phosphate-binding protein (PBP-1) of an ABC-type phosphate transporter from Clostridium perfringens.

Author information

1
URMITE UMR CNRS-IRD 6236, IFR48, Faculté de Médecine et de Pharmacie, Université de la Méditerranée, Marseille, France.
2
1] URMITE UMR CNRS-IRD 6236, IFR48, Faculté de Médecine et de Pharmacie, Université de la Méditerranée, Marseille, France [2] University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics &Biotechnology Institute, St. Paul, MN 55108, USA.
3
University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics &Biotechnology Institute, St. Paul, MN 55108, USA.

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.

PMID:
25338617
PMCID:
PMC5381212
DOI:
10.1038/srep06636
[Indexed for MEDLINE]
Free PMC Article

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