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- PDB-9uu5: Cryo-EM structure of the maize CER6-GL2 complex in the presence o... -

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Basic information

Entry
Database: PDB / ID: 9uu5
TitleCryo-EM structure of the maize CER6-GL2 complex in the presence of 30:0 CoA
Components
  • 3-ketoacyl-CoA synthase
  • Protein ECERIFERUM 26-like
KeywordsPLANT PROTEIN / Complex / 30:0 CoA
Function / homology
Function and homology information


fatty acid elongase activity / acyltransferase activity, transferring groups other than amino-acyl groups / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / fatty acid biosynthetic process / membrane
Similarity search - Function
Very-long-chain 3-ketoacyl-CoA synthase / FAE1/Type III polyketide synthase-like protein / FAE1/Type III polyketide synthase-like protein / : / Transferase family / 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III, C-terminal / 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal / Chloramphenicol acetyltransferase-like domain superfamily / Thiolase-like
Similarity search - Domain/homology
Protein ECERIFERUM 26-like / 3-ketoacyl-CoA synthase
Similarity search - Component
Biological speciesZea mays (maize)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.26 Å
AuthorsLiu, Y. / Zhang, P.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32230050 China
CitationJournal: Sci Adv / Year: 2025
Title: Molecular basis of very-long-chain fatty acid elongation by the CER6-GL2 enzyme complex in plant wax biosynthesis.
Authors: Yaqi Liu / Yuan Chen / Xue Zhang / Mengxue Li / Ji Wang / Zhao Yang / Miaolian Ma / Zhiwei Zhao / Hongtao Liu / Fang Yu / Peng Zhang /
Abstract: Plant cuticular waxes, crucial hydrophobic barriers, are primarily composed of aliphatics derived from very-long-chain fatty acids (VLCFAs; >C28) synthesized by the endoplasmic reticulum fatty acid ...Plant cuticular waxes, crucial hydrophobic barriers, are primarily composed of aliphatics derived from very-long-chain fatty acids (VLCFAs; >C28) synthesized by the endoplasmic reticulum fatty acid elongase complex. The core catalytic subunit, CER6 (KCS6), requires interaction with the BAHD protein GL2 to elongate acyl chains beyond C28. We determined the cryo-electron microscopy structure of the maize CER6-GL2 (ZmCER6-ZmGL2) heterotetramer bound to coenzyme A (CoA) and malonyl-CoA, revealing a membrane-anchored ZmCER6 homodimer, with each cytosolic catalytic domain having a substrate tunnel. Structural and biochemical analyses suggest that ZmGL2's amino terminus binds ZmCER6 and remodels its substrate tunnel into a continuous hydrophobic channel at their interface, enabling acyl-chain elongation. CER6 uses a distinct Cys-His-Asn catalytic triad, differing from the histidine-dependent catalysis of mammalian elongases. GL2 acts noncatalytically to modulate CER6 activity. Comparative analyses suggest that species-specific substrate preferences arise from divergent CER2/GL2 interactions. This work elucidates the acyl-chain elongation mechanism of plant VLCFA biosynthesis and provides a foundation for engineering stress-resilient crops via wax modulation.
History
DepositionMay 5, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Oct 29, 2025Provider: repository / Type: Initial release
Revision 1.0Oct 29, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Oct 29, 2025Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Oct 29, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
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Revision 1.1Mar 11, 2026Group: Data collection / Database references / Category: citation / citation_author / em_admin
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Protein ECERIFERUM 26-like
B: 3-ketoacyl-CoA synthase
D: Protein ECERIFERUM 26-like
C: 3-ketoacyl-CoA synthase


Theoretical massNumber of molelcules
Total (without water)206,5574
Polymers206,5574
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Protein ECERIFERUM 26-like / GL2


Mass: 46864.980 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Zea mays (maize) / Gene: LOC103645956 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: A0A804MAL4
#2: Protein 3-ketoacyl-CoA synthase / CER6


Mass: 56413.438 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Zea mays (maize) / Gene: LOC100191595, ZEAMMB73_Zm00001d028241 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: B4G0N2, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Cryo-EM structure of the maize CER6-GL2 complex in the presence of 30:0 CoA
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Zea mays (maize)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 7.5
SpecimenConc.: 10 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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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: 2200 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 58.3 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.14_3260: / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.26 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 207945 / Symmetry type: POINT

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