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- PDB-9tlk: Cryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes HF-25 -

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Basic information

Entry
Database: PDB / ID: 9tlk
TitleCryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes HF-25
ComponentsProtochlorophyllide reductase B, chloroplastic
KeywordsPHOTOSYNTHESIS / photoenzyme / chlorophyllide / oligomer
Function / homology
Function and homology information


protochlorophyllide reductase / protochlorophyllide reductase activity / response to ethylene / chlorophyll biosynthetic process / chloroplast outer membrane / chloroplast thylakoid / chloroplast envelope / chloroplast thylakoid membrane / photosynthesis / chloroplast ...protochlorophyllide reductase / protochlorophyllide reductase activity / response to ethylene / chlorophyll biosynthetic process / chloroplast outer membrane / chloroplast thylakoid / chloroplast envelope / chloroplast thylakoid membrane / photosynthesis / chloroplast / protein domain specific binding / mRNA binding / cytosol
Similarity search - Function
Light-dependent protochlorophyllide reductase / short chain dehydrogenase / Short-chain dehydrogenase/reductase SDR / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
: / 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE / Chem-NDP / Protochlorophyllide reductase B, chloroplastic
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsGabruk, M. / Desfosses, A. / Estrozi, L.F. / Pintscher, S. / Rawski, M.
Funding support Poland, 1items
OrganizationGrant numberCountry
Polish National Science Centre2019/35/D/NZ1/00295 Poland
CitationJournal: Nat Commun / Year: 2026
Title: Structures of LPOR-Chlide complexes reveal the structural basis of membrane remodeling and photocatalysis
Authors: Gabruk, M. / Desfosses, A. / Estrozi, L.F. / Pintscher, S. / Rawski, M. / Wazny, G. / Garbacz, A. / Zbyradowski, M. / Kruk, J. / Fiedor, L.
History
DepositionDec 10, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 12, 2026Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
AA: Protochlorophyllide reductase B, chloroplastic
AB: Protochlorophyllide reductase B, chloroplastic
AC: Protochlorophyllide reductase B, chloroplastic
AD: Protochlorophyllide reductase B, chloroplastic
AE: Protochlorophyllide reductase B, chloroplastic
AF: Protochlorophyllide reductase B, chloroplastic
AG: Protochlorophyllide reductase B, chloroplastic
AH: Protochlorophyllide reductase B, chloroplastic
AI: Protochlorophyllide reductase B, chloroplastic
AJ: Protochlorophyllide reductase B, chloroplastic
AK: Protochlorophyllide reductase B, chloroplastic
AL: Protochlorophyllide reductase B, chloroplastic
BA: Protochlorophyllide reductase B, chloroplastic
BB: Protochlorophyllide reductase B, chloroplastic
BC: Protochlorophyllide reductase B, chloroplastic
BD: Protochlorophyllide reductase B, chloroplastic
BE: Protochlorophyllide reductase B, chloroplastic
BF: Protochlorophyllide reductase B, chloroplastic
BG: Protochlorophyllide reductase B, chloroplastic
BH: Protochlorophyllide reductase B, chloroplastic
BI: Protochlorophyllide reductase B, chloroplastic
BJ: Protochlorophyllide reductase B, chloroplastic
BK: Protochlorophyllide reductase B, chloroplastic
BL: Protochlorophyllide reductase B, chloroplastic
CA: Protochlorophyllide reductase B, chloroplastic
CB: Protochlorophyllide reductase B, chloroplastic
CC: Protochlorophyllide reductase B, chloroplastic
CD: Protochlorophyllide reductase B, chloroplastic
CE: Protochlorophyllide reductase B, chloroplastic
CF: Protochlorophyllide reductase B, chloroplastic
CG: Protochlorophyllide reductase B, chloroplastic
CH: Protochlorophyllide reductase B, chloroplastic
CI: Protochlorophyllide reductase B, chloroplastic
CJ: Protochlorophyllide reductase B, chloroplastic
CK: Protochlorophyllide reductase B, chloroplastic
CL: Protochlorophyllide reductase B, chloroplastic
DA: Protochlorophyllide reductase B, chloroplastic
DB: Protochlorophyllide reductase B, chloroplastic
DC: Protochlorophyllide reductase B, chloroplastic
DD: Protochlorophyllide reductase B, chloroplastic
DE: Protochlorophyllide reductase B, chloroplastic
DF: Protochlorophyllide reductase B, chloroplastic
DG: Protochlorophyllide reductase B, chloroplastic
DH: Protochlorophyllide reductase B, chloroplastic
DI: Protochlorophyllide reductase B, chloroplastic
DJ: Protochlorophyllide reductase B, chloroplastic
DK: Protochlorophyllide reductase B, chloroplastic
DL: Protochlorophyllide reductase B, chloroplastic
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,938,426192
Polymers1,835,34448
Non-polymers103,082144
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein ...
Protochlorophyllide reductase B, chloroplastic / PCR B / NADPH-protochlorophyllide oxidoreductase B / POR B


Mass: 38236.324 Da / Num. of mol.: 48
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: PORB, At4g27440, F27G19.40 / Plasmid: pET15b / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): pRIL / References: UniProt: P21218, protochlorophyllide reductase
#2: Chemical...
ChemComp-NDP / NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE


Mass: 745.421 Da / Num. of mol.: 48 / Source method: obtained synthetically / Formula: C21H30N7O17P3 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical...
ChemComp-LMG / 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE


Mass: 787.158 Da / Num. of mol.: 48 / Source method: obtained synthetically / Formula: C45H86O10 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical...
ChemComp-A1JWG / Chlorophyllide a


Mass: 614.973 Da / Num. of mol.: 48 / Source method: obtained synthetically / Formula: C35H34MgN4O5 / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: HELICAL ARRAY / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: Cryo-EM Structure of the oligomeric LPOR:Chlide:NADPH Complexes HF-25
Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Source (recombinant)Organism: Escherichia coli (E. coli) / Strain: BL21(DE3)pRIL / Plasmid: pET15b
Buffer solutionpH: 7.1
Buffer component
IDConc.NameFormulaBuffer-ID
137 mMsodium phosphateNa2HPO41
2225 mMsodium chlorideNaCl1
3150 mMimidazoleimidazole1
45 mM2-mercaptoethanol2-mercaptoethanol1
525 %glycerolglycerol1
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Details: 28 uM AtPORB, 40 uM Chlorophyllide, 600 uM NADPH, 230 uM lipids (50mol% MGDG, 35mol% DGDG, 15mol% PG)
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 294 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2100 nm / Nominal defocus min: 900 nm
Image recordingElectron dose: 40 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARC4.3particle selection
9PHENIX1.21.2_5419model refinement
13cryoSPARC4.33D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: -114.391 ° / Axial rise/subunit: 25.609 Å / Axial symmetry: D4
3D reconstructionResolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 23139 / Symmetry type: HELICAL
Atomic model buildingPDB-ID: 7JK9

7jk9


Accession code: 7JK9 / Details: initial model / Source name: PDB / Type: experimental model

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