The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol
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 (...
| Main Authors: | , , , , , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2022
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| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/161179 |
| _version_ | 1826113510900236288 |
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| author | He, Qinghua Toh, Joel Dewei Ero, Rya Qiao, Zhu Kumar, Veerendra Serra, Aida Tan, Jackie Sze, Siu Kwan Gao, Yong-Gui |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences He, Qinghua Toh, Joel Dewei Ero, Rya Qiao, Zhu Kumar, Veerendra Serra, Aida Tan, Jackie Sze, Siu Kwan Gao, Yong-Gui |
| author_sort | He, Qinghua |
| collection | NTU |
| description | 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 (DsGPDH) protein featuring a phosphoserine phosphatase-like domain fused to the canonical glycerol-3-phosphate (G3P) dehydrogenase domain. Biochemical assays confirm that DsGPDH 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 DsGPDH 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. |
| first_indexed | 2024-10-01T03:24:26Z |
| format | Journal Article |
| id | ntu-10356/161179 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T03:24:26Z |
| publishDate | 2022 |
| record_format | dspace |
| spelling | ntu-10356/1611792022-08-17T08:38:51Z The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol He, Qinghua Toh, Joel Dewei Ero, Rya Qiao, Zhu Kumar, Veerendra Serra, Aida Tan, Jackie Sze, Siu Kwan Gao, Yong-Gui School of Biological Sciences NTU Institute of Structural Biology Science::Biological sciences Dunaliella Salt-Resistance 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 (DsGPDH) protein featuring a phosphoserine phosphatase-like domain fused to the canonical glycerol-3-phosphate (G3P) dehydrogenase domain. Biochemical assays confirm that DsGPDH 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 DsGPDH 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. Ministry of Education (MOE) This work was supported by a Tier II grants MOE2014-T2-1-083 from the Ministry of Education of Singapore and a NIMBELS from NTU. QH was supported by the Fundamental Research Funds for the Central Universities, Southwest Minzu University (2017NZYQN36). 2022-08-17T08:36:25Z 2022-08-17T08:36:25Z 2020 Journal Article He, Q., Toh, J. D., Ero, R., Qiao, Z., Kumar, V., Serra, A., Tan, J., Sze, S. K. & Gao, Y. (2020). The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol. The Plant Journal, 102(1), 153-164. https://dx.doi.org/10.1111/tpj.14619 0960-7412 https://hdl.handle.net/10356/161179 10.1111/tpj.14619 31762135 2-s2.0-85077168326 1 102 153 164 en MOE2014-T2-1-083 The Plant Journal © 2019 The Authors. All rights reserved. |
| spellingShingle | Science::Biological sciences Dunaliella Salt-Resistance He, Qinghua Toh, Joel Dewei Ero, Rya Qiao, Zhu Kumar, Veerendra Serra, Aida Tan, Jackie Sze, Siu Kwan Gao, Yong-Gui 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 |
| title_full | The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol |
| title_fullStr | The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol |
| title_full_unstemmed | The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol |
| title_short | The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol |
| title_sort | unusual di domain structure of dunaliella salina glycerol 3 phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol |
| topic | Science::Biological sciences Dunaliella Salt-Resistance |
| url | https://hdl.handle.net/10356/161179 |
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