A novel opportunity to combat the global Phosphorus crisis: investigating structure function relationships of an atypical phosphatase in soil bacteria

Humanity is facing several threats to global food security, one of which is the emerging global phosphorus crisis that has resulted from the imbalance in global application of phosphate fertilisers. For a sustainable and continued existence, humanity urgently needs to improve the efficiency by which plants and animals acquire phosphorus from soils or feed, respectively.
Phosphorus exists in many inorganic and organic forms. Organisms typically need phosphorus to be in a simple inorganic form phosphate. Unfortunately, most phosphorus is found in an organic pool and enzymes called phosphatases are required to release the bioavailable phosphate.
We recently identified a highly active and functionally unique phosphatase (PafA) in a group of environmental bacteria that outperforms previously characterised phosphatases from different enzyme families. PafA variants associated with the rhizosphere may represent the most active phosphatases, despite appearing to possess identical catalytic residues.
This project will investigate structure-function relationships in PafA using protein biochemistry, site-directed mutagenesis and structural biology. The student will characterise PafA from Flavobacterium johnsoniae as the model and compare this with distinct PafA rhizosphere variants identified through next-generation sequencing. This work will characterise a key new enzyme in global phosphorus cycling, which presents an exciting solution for enhancing sustainable agriculture.