We provide the first experimental analysis of AGT structural dynamics, showing that stability is heterogeneous in the native state and providing a blueprint for frustrated regions with potentially functional relevance.

 Mutations in alanine:glyoxylate aminotransferase (AGT) leading to protein misfolding cause primary hyperoxaluria type I (PH1). Here, we use hydrogen-deuterium exchange to characterize the structural dynamics of AGT variants. These dynamics are heterogeneously distributed across the structure and different functional sites. Disease-associated variants show local destabilization. Our work provides novel insight into the pathogenic mechanisms causing PH1. This work has been published in FEBS Letters here: