Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of dynamic P5CS filaments.
Journal, issue, pages	Elife, Vol. 11, Year 2022
Publish date	Mar 14, 2022
Authors	Jiale Zhong / Chen-Jun Guo / Xian Zhou / Chia-Chun Chang / Boqi Yin / Tianyi Zhang / Huan-Huan Hu / Guang-Ming Lu / Ji-Long Liu /
PubMed Abstract	The bifunctional enzyme Δ-pyrroline-5-carboxylate synthase (P5CS) is vital to the synthesis of proline and ornithine, playing an essential role in human health and agriculture. Pathogenic mutations ...The bifunctional enzyme Δ-pyrroline-5-carboxylate synthase (P5CS) is vital to the synthesis of proline and ornithine, playing an essential role in human health and agriculture. Pathogenic mutations in the P5CS gene (ALDH18A1) lead to neurocutaneous syndrome and skin relaxation connective tissue disease in humans, and P5CS deficiency seriously damages the ability to resist adversity in plants. We have recently found that P5CS forms cytoophidia in vivo and filaments in vitro. However, it is difficult to appreciate the function of P5CS filamentation without precise structures. Using cryo-electron microscopy, here we solve the structures of full-length P5CS in three states at resolution from 3.1 to 4.3 Å. We observe distinct ligand-binding states and conformational changes for the GK and GPR domains, respectively. Divergent helical filaments are assembled by P5CS tetramers and stabilized by multiple interfaces. Point mutations disturbing those interfaces prevent P5CS filamentation and greatly reduce the enzymatic activity. Our findings reveal that filamentation is crucial for the coordination between the GK and GPR domains, providing a structural basis for the catalytic function of P5CS filaments.
External links	Elife / PubMed:35286254 / PubMed Central
Methods	EM (single particle)
Resolution	3.1 - 4.3 Å
Structure data	31466 7f5t EMDB-31466: Structural basis of assembly and activity of P5CS filament PDB-7f5t: Drosophila P5CS filament with glutamate Method: EM (single particle) / Resolution: 4.1 Å 31467 7f5u EMDB-31467, PDB-7f5u: Drosophila P5CS filament with glutamate and ATPgammaS Method: EM (single particle) / Resolution: 4.1 Å 31468 7f5v EMDB-31468, PDB-7f5v: Drosophila P5CS filament with glutamate, ATP, and NADPH Method: EM (single particle) / Resolution: 3.6 Å 31469 7f5x EMDB-31469, PDB-7f5x: GK domain of Drosophila P5CS filament with glutamate Method: EM (single particle) / Resolution: 3.5 Å 32875 7wx3 EMDB-32875, PDB-7wx3: GK domain of Drosophila P5CS filament with glutamate, ATP, and NADPH Method: EM (single particle) / Resolution: 3.1 Å 32876 7wx4 EMDB-32876, PDB-7wx4: GK domain of Drosophila P5CS filament with glutamate and ATPgammaS Method: EM (single particle) / Resolution: 3.4 Å 32877 7wxf EMDB-32877, PDB-7wxf: GPR domain of Drosophila P5CS filament with glutamate Method: EM (single particle) / Resolution: 3.6 Å 32878 7wxg EMDB-32878, PDB-7wxg: GPR domain closed form of Drosophila P5CS filament with glutamate, ATP, and NADPH Method: EM (single particle) / Resolution: 4.2 Å 32879 7wxh EMDB-32879, PDB-7wxh: GPR domain open form of Drosophila P5CS filament with glutamate, ATP, and NADPH Method: EM (single particle) / Resolution: 4.3 Å 32880 7wxi EMDB-32880, PDB-7wxi: GPR domain of Drosophila P5CS filament with glutamate and ATPgammaS Method: EM (single particle) / Resolution: 4.2 Å
Chemicals	ChemComp-GLU: GLUTAMIC ACID ChemComp-GGL: GAMMA-L-GLUTAMIC ACID ChemComp-RGP: GAMMA-GLUTAMYL PHOSPHATE ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-NAP*: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
Source	drosophila melanogaster (fruit fly)
Keywords	TRANSFERASE / glutamate-bound / filament / ALDH18A1 / Delta-1-pyrroline-5-carboxylate synthase / BIOSYNTHETIC PROTEIN