8haw | pdb_00008haw

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

spinqualitylabelsall models 8haw, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8haw is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CA, GOL, PO4, TPO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NPC4_ARATH Non-specific phospholipase C (PLC) which assumes major PLC activity during inorganic phosphate starvation. Substrate preference is phosphatidylcholine (PC), but can also hydrolyze phosphatidylethanolamine (PE) with lower efficiency. Has no activity toward phosphatidic acid (PA). Plays an important role in the supply of both inorganic phosphate and diacylglycerol from membrane-localized phospholipids during phosphate deprivation. May be required for lipid-derived signaling molecules that positively modulate abscisic acid (ABA) response and promote plant tolerance to drought and salt stresses. May be involved in brassinolide-mediated signaling in root development. Publication Abstract from PubMed 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 A. 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(alpha1)-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. Insights into the mechanism of phospholipid hydrolysis by plant non-specific phospholipase C.,Fan R, Zhao F, Gong Z, Chen Y, Yang B, Zhou C, Zhang J, Du Z, Wang X, Yin P, Guo L, Liu Z Nat Commun. 2023 Jan 12;14(1):194. doi: 10.1038/s41467-023-35915-4. PMID:36635324 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phospholipase C

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