7EOZ

The structure of rice Defective Pollen Wall (DPW) in the complex with its cofactor NADP

Summary for 7EOZ

• Entry DOI: 10.2210/pdb7eoz/pdb
• Descriptor: Fatty acyl-CoA reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: fatty acyl carrier protein reductase, udp-glucose epimerase, lipid and sugar metabolisms, nadp+, plant, lipid binding protein, oxidoreductase
• Biological source: Oryza sativa Japonica Group (Japanese rice)
• Total number of polymer chains: 2
• Total formula weight: 117413.98

Authors

Yan, L.M.,Wang, W.,Li, G.,Wang, J. (deposition date: 2021-04-24, release date: 2022-08-24, Last modification date: 2025-03-19)

Primary citation

Qu, S.,Wang, J.,Li, G.,Miao, C.,Yan, L.,Wang, W.
Structural basis for the dual roles of DPW in lipid and UDP-sugar metabolism during rice anther development.
Plant Physiol Biochem., 222:109762-109762, 2025

PubMed Abstract: Fatty acids and uridine diphosphate (UDP)-sugars are essential metabolites involved in the biosynthesis of polysaccharides and lipids, both of which are critical for anther development in plants. Our previous study identified Defective Pollen Wall (DPW), a rice fatty acyl carrier protein reductase (FAR), as a key factor in pollen wall formation. In this study, we demonstrate that the structure of DPW in complex with its cofactor NADP exhibits structural similarities to that of UDP-glucose epimerase (UGE). In vitro enzymatic assays utilizing recombinant DPW confirmed its ability to interconvert UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal) in an NADP(H)-dependent manner. Mutations in conserved NADP(H)-binding residues abolished both DPW's FAR and UGE activities. In vivo assays showed that the dpw mutation causes UDP-Glc accumulation, disrupting the balance between UDP-Glc and UDP-Gal in rice anthers. Taken together, our findings provide insights into the dual roles of DPW in lipid and UDP-sugar metabolism during rice anther development, shedding light on how plants integrate metabolic pathways through multifunctional enzymes to regulate male reproductive development.

PubMed: 40068458
DOI: 10.1016/j.plaphy.2025.109762

Experimental method

X-RAY DIFFRACTION (3.4 Å)