High resolution structural and functional analysis of a hemopexin motif protein from Dolichos

The high-resolution crystal structure of DC25, a 2S albumin protein from Dolichos, at 1.28 Å resolution is reported. The protein has β-propeller structure with a central channel containing only water molecules while the proteins having similar folds have ions along with water or ions only. The four conserved water molecules were found between the blades which help to maintain its tertiary structure. We also discovered the intrinsic peroxidase activity of DC25 which could be inhibited by a heme analog. Our study sheds light on the physiological role of DC25 which may acts as a detoxifying agent to relieve the germinating seed from oxidative stress.

Full article: https://www.nature.com/articles/s41598-019-56257-6


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