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	Structures of LPOR-Chlide complexes reveal the structural basis of membrane remodeling and photocatalysis.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Year 2026
Publish date	Aug 5, 2026
Authors	Michał Gabruk / Ambroise Desfosses / Leandro Farias Estrozi / Sebastian Pintscher / Michał Rawski / Grzegorz Ważny / Agnieszka Garbacz / Mateusz Zbyradowski / Jerzy Kruk / Leszek Fiedor /
PubMed Abstract	Light-dependent protochlorophyllide oxidoreductase (LPOR) is a light-driven enzyme in flowering plants. It is involved in chlorophyll biosynthesis while also reorganizing membrane lipids into the ...Light-dependent protochlorophyllide oxidoreductase (LPOR) is a light-driven enzyme in flowering plants. It is involved in chlorophyll biosynthesis while also reorganizing membrane lipids into the cubic membrane network that supports chloroplast development. However, the structural basis of these two activities and their relationship have remained unclear. Here, cryo-electron microscopy of chlorophyllide-bound LPOR oligomers reveals nine distinct assembly states, including helical filaments, stacked rings and segmented strings of dimers. We find that strings of LPOR dimers reshape lipid bilayers into a range of membrane architectures through combinations of three inter-string interfaces, providing a structural explanation for the flexibility of these assemblies. The highest-resolution map (2.55 Å), shows the pigment-binding region in sufficient detail to reveal a solvent-accessible channel near the pigment and a conformation of the propionate group may support hydride transfer from NADPH. Together, these findings establish a structural framework linking LPOR oligomerization, membrane remodeling and photocatalysis, and suggest that chlorophyllide-bound LPOR assemblies may have a regulatory function in mature leaves.
External links	Nat Commun / PubMed:42686771 / PubMed Central
Methods	EM (helical sym.)
Resolution	2.55 - 3.87 Å
Structure data	56043 9tl6 EMDB-56043, PDB-9tl6: Cryo-EM Structure of the LPOR:Chlide:NADPH Complexes (RD-21) - improved resolution of a dimer building block form RF-21 Method: EM (helical sym.) / Resolution: 2.64 Å 56044 9tl7 EMDB-56044, PDB-9tl7: Cryo-EM Structure of the LPOR:Chlide:NADPH Complexes (RD-23) - improved resolution of a dimer building block form RF-23 Method: EM (helical sym.) / Resolution: 2.66 Å 56045 9tl8 EMDB-56045, PDB-9tl8: Cryo-EM Structure of the LPOR:Chlide:NADPH Complexes (RD-A) - improved resolution of a dimer building block form RF-21, RF-23 and RF-25 Method: EM (helical sym.) / Resolution: 2.55 Å 56046 9tl9 EMDB-56046, PDB-9tl9: Cryo-EM Structure of the LPOR:Chlide:NADPH Complexes (RD-25) - improved resolution of a dimer building block form RF-25 Method: EM (helical sym.) / Resolution: 2.58 Å 56047 9tla EMDB-56047, PDB-9tla: Cryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes RF-21 Method: EM (helical sym.) / Resolution: 3.17 Å 56048 9tlb EMDB-56048, PDB-9tlb: Cryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes RF-23 Method: EM (helical sym.) / Resolution: 3.2 Å 56049 9tlc EMDB-56049, PDB-9tlc: Cryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes RF-25 Method: EM (helical sym.) / Resolution: 3.2 Å EMDB-56050: Cryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes SF-25 Method: EM (helical sym.) / Resolution: 3.8 Å EMDB-56051: Cryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes HF-29 Method: EM (helical sym.) / Resolution: 3.87 Å 56055 9tlh EMDB-56055, PDB-9tlh: Cryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes HF-23 Method: EM (helical sym.) / Resolution: 3.03 Å 56056 9tlk EMDB-56056, PDB-9tlk: Cryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes HF-25 Method: EM (helical sym.) / Resolution: 3.2 Å
Chemicals	ChemComp-NDP: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE PDB-1jwg: VHS Domain of human GGA1 complexed with cation-independent M6PR C-terminal Peptide ChemComp-LMG: 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE ChemComp-HOH: WATER
Source	arabidopsis thaliana (thale cress)
Keywords	PHOTOSYNTHESIS / photoenzyme / chlorophyllide / oligomer