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Sharma, Sarita Chandan and Kumar, Ashish and Vashisht, Sharad and Salunke, Dinakar M. (2020) Publisher Correction: High resolution structural and functional analysis of a hemopexin motif protein from Dolichos. Scientific Reports, 10 (1). ISSN 2045-2322

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Publisher Correction High Resolution Structural and Functional Analysis of a Hemopexin Motif Protein From Dolichos.pdf
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It is increasingly evident that seed proteins exhibit specifc functions in plant physiology. However, many proteins remain yet to be functionally characterized. We have screened the seed proteome of Dolichos which lead to identifcation and purifcation of a protein, DC25. The protein was monomeric and highly thermostable in extreme conditions of pH and salt. It was crystallized and structure determined at 1.28Å resolution using x-ray crystallography. The high-resolution structure of the protein revealed a four-bladed β-propeller hemopexin-type fold containing pseudo four-fold molecular symmetry at the central channel. While the structure exhibited homology with 2S albumins, variations in the loops connecting the outermost strands and the diferences in surface-charge distribution may be relevant for distinct functions. Comparative study of the protein with other seed hemopexins revealed the presence of four conserved water molecules in between the blades which cross-link them and maintain the tertiary structure. The protein exhibited intrinsic peroxidase activity, which could be inhibited by binding of a heme analog. The identifcation of redox-sensitive cysteine and inhibition of peroxidase activity by iodoacetamide facilitated characterization of the possible active site. The determined peroxidase activity of DC25 may be responsible for rescuing germinating seeds from oxidative stress.

Item Type: Article
Subjects: Biochemical and Biophysical Sciences
Agriculture and Environment
Depositing User: RCB Library
Date Deposited: 25 Jun 2020 12:01
Last Modified: 25 Jun 2020 12:01
URI: http://rcb.sciencecentral.in/id/eprint/217

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