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A metal ion–dependent conformational switch modulates activity of the Plasmodium M17 aminopeptidase 1 Results 2 Hexameric assembly stabilizes and links the PfA-M17 active sites 2 Novel PfA-M17 conformation captured by crystallography 3 In situ crystalline protein dynamics observed in PfA-M17 5 Asp394 implicated in the formation of the catalytically competent active site in PfA-M17 5 Dynamic loop regulates PfA-M17 catalysis 6 Regulatory loop differs throughout M17 aminopeptidase family 7 Discussion 7 Conclusion 9 Experimental procedures 9 Molecular biology, protein production, and purification 9 Aminopeptidase assays and analysis 9 Crystallization, data collection, structure determination, and refinement 10 MD system setup and simulation protocol 10 MD analysis 11 Data availability 11 Supporting information 11 Author contributions 11 Funding and additional information 11 References 11
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