The unusual di‐domain structure of Dunaliella salina glycerol‐3‐phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol

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The unusual di‐domain structure of Dunaliella salina glycerol‐3‐phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol
Title:
The unusual di‐domain structure of Dunaliella salina glycerol‐3‐phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol
Journal Title:
The Plant Journal
Keywords:
Publication Date:
24 November 2019
Citation:
He, Q., Toh, J.D., Ero, R., Qiao, Z., Kumar, V., Serra, A., Tan, J., Sze, S.K. and Gao, Y.‐G. (2020), The unusual di‐domain structure of Dunaliella salina glycerol‐3‐phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol. Plant J, 102: 153-164. doi:10.1111/tpj.14619
Abstract:
Dunaliella has been extensively studied due to its intriguing adaptation to high salinity. Its di‐domain glycerol‐3‐phosphate dehydrogenase (GPDH) isoform is likely to underlie the rapid production of the osmoprotectant glycerol. Here, we report the structure of the chimeric Dunaliella salina GPDH (Ds GPDH) protein featuring a phosphoserine phosphatase‐like domain fused to the canonical glycerol‐3‐phosphate (G3P) dehydrogenase domain. Biochemical assays confirm that Ds GPDH can convert dihydroxyacetone phosphate (DHAP) directly to glycerol, whereas a separate phosphatase protein is required for this conversion process in most organisms. The structure of Ds GPDH in complex with its substrate DHAP and co‐factor nicotinamide adenine dinucleotide (NAD) allows the identification of the residues that form the active sites. Furthermore, the structure reveals an intriguing homotetramer form that likely contributes to the rapid biosynthesis of glycerol.
License type:
PublisherCopyrights
Funding Info:
Ministry of Education ‐ Singapore, Grant Number: MOE2014‐T2‐1‐083; Southwest Minzu University, Grant Number: 2017NZYQN36; Nanyang Technological University, Grant Number: NIM/01/2018; Ministry of Education, Grant Number: 2017NZYQN36
Description:
This is the peer reviewed version of the following article: He, Q., Toh, J.D., Ero, R., Qiao, Z., Kumar, V., Serra, A., Tan, J., Sze, S.K. and Gao, Y.‐G. (2020), The unusual di‐domain structure of Dunaliella salina glycerol‐3‐phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol. Plant J, 102: 153-164. doi:10.1111/tpj.14619, which has been published in final form at https://doi.org/10.1111/tpj.14619. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
ISSN:
1365-313X
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