NMR experiments redefine the hemoglobin binding properties of bacterial NEAr-iron Transporter domains.

ABSTRACT: Iron is a versatile metal cofactor that is used in a wide range of essential cellular processes. During infections, many bacterial pathogens acquire iron from human hemoglobin (Hb), which contains the majority of the body's total iron content in the form of heme (iron protoporphyrin IX). Clinically important Gram-positive bacterial pathogens scavenge heme using an array of secreted and cell-wall-associated receptors that contain NEAr-iron Transporter (NEAT) domains. Experimentally defining the Hb binding properties of NEAT domains has been challenging, limiting our understanding of their function in heme uptake. Here we show that solution-state NMR spectroscopy is a powerful tool to define the Hb binding properties of NEAT domains. The utility of this method is demonstrated using the NEAT

SUBMITTER: Macdonald R 

PROVIDER: S-EPMC6635774 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature