8HAW

An auto-activation mechanism of plant non-specific phospholipase C

Summary for 8HAW

• Entry DOI: 10.2210/pdb8haw/pdb
• Descriptor: Non-specific phospholipase C4, PHOSPHATE ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: npc4, non-specific phospholipase c, glycosylinositolphosphorylceramide, phosphatidylcholine, hydrolase
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 112070.66

Authors

Zhao, F.,Fan, R.Y.,Guan, Z.Y.,Guo, L.,Yin, P. (deposition date: 2022-10-26, release date: 2023-01-25, Last modification date: 2024-10-23)

Primary citation

Fan, R.,Zhao, F.,Gong, Z.,Chen, Y.,Yang, B.,Zhou, C.,Zhang, J.,Du, Z.,Wang, X.,Yin, P.,Guo, L.,Liu, Z.
Insights into the mechanism of phospholipid hydrolysis by plant non-specific phospholipase C.
Nat Commun, 14:194-194, 2023

PubMed Abstract: Non-specific phospholipase C (NPC) hydrolyzes major membrane phospholipids to release diacylglycerol (DAG), a potent lipid-derived messenger regulating cell functions. Despite extensive studies on NPCs reveal their fundamental roles in plant growth and development, the mechanistic understanding of phospholipid-hydrolyzing by NPCs, remains largely unknown. Here we report the crystal structure of Arabidopsis NPC4 at a resolution of 2.1 Å. NPC4 is divided into a phosphoesterase domain (PD) and a C-terminal domain (CTD), and is structurally distinct from other characterized phospholipases. The previously uncharacterized CTD is indispensable for the full activity of NPC4. Mechanistically, CTD contributes NPC4 activity mainly via CTD-PD interaction, which ultimately stabilizes the catalytic pocket in PD. Together with a series of structure-guided biochemical studies, our work elucidates the structural basis and provides molecular mechanism of phospholipid hydrolysis by NPC4, and adds new insights into the members of phospholipase family.

PubMed: 36635324
DOI: 10.1038/s41467-023-35915-4

Experimental method

X-RAY DIFFRACTION (2.1 Å)