6iuy

Structure of DsGPDH of Dunaliella salina

spinqualitylabelsall models 6iuy, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6iuy is a 2 chain structure with sequence from Dunaliella salina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: 13P, GOL, MG, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q52ZA0_DUNSA Publication Abstract from PubMed Dunaliella has been extensively studied due to its intriguing adaptation to high salinity. Its di-domain glycerol-3-phosphate dehydrogenase (GPDH) isoform likely underlies 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 cofactor 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. The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol.,He Q, Toh JD, Ero R, Qiao Z, Kumar V, Serra A, Tan J, Sze SK, Gao YG Plant J. 2019 Nov 24. doi: 10.1111/tpj.14619. PMID:31762135 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycerol-3-phosphate dehydrogenase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA