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

Daniel Gonzalez, Magali Richez, Celine Bergonzi, Eric Chabriere, Mikael H Elias

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

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.

Original languageEnglish (US)
Article number6636
JournalScientific reports
Volume4
DOIs
StatePublished - Oct 16 2014

Bibliographical note

Funding Information:
This research was supported by a grant to EC from ‘‘Agence Nationale pour la Recherche sur le Sida et les Hépatites Virales’’ (grant Nu12264). M.R. and D.G. were supported by grants from AP-HM (Marseille, France).

Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.

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