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- EMDB-65382: Cryo-EM structure of the erlin1/2 complex purified using DDM and GDN -

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Open data


ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-65382
TitleCryo-EM structure of the erlin1/2 complex purified using DDM and GDN
Map data
Sample
  • Complex: The erlin1/2 complex
    • Protein or peptide: Erlin-1
    • Protein or peptide: Erlin-2
KeywordsCryo-EM / complex / MEMBRANE PROTEIN / SPFH protein family
Function / homology
Function and homology information


regulation of cholesterol biosynthetic process / Signaling by plasma membrane FGFR1 fusions / SREBP signaling pathway / negative regulation of cholesterol biosynthetic process / negative regulation of fatty acid biosynthetic process / cholesterol binding / cholesterol metabolic process / ERAD pathway / Signaling by FGFR1 in disease / Defective CFTR causes cystic fibrosis ...regulation of cholesterol biosynthetic process / Signaling by plasma membrane FGFR1 fusions / SREBP signaling pathway / negative regulation of cholesterol biosynthetic process / negative regulation of fatty acid biosynthetic process / cholesterol binding / cholesterol metabolic process / ERAD pathway / Signaling by FGFR1 in disease / Defective CFTR causes cystic fibrosis / ABC-family proteins mediated transport / membrane raft / ubiquitin protein ligase binding / endoplasmic reticulum membrane / endoplasmic reticulum / protein-containing complex / plasma membrane / cytosol
Similarity search - Function
Erlin1/2 / Band 7 domain / SPFH domain / Band 7 family / prohibitin homologues / Band 7/SPFH domain superfamily
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.6 Å
AuthorsYan L / Gao N
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)92354306 China
CitationJournal: Mol.Cell / Year: 2026
Title: The Erlin1/2 complex is a dynamic scaffold for membrane microdomain assembly on the endoplasmic reticulum
Authors: Yan L / Gao N
History
DepositionJul 15, 2025-
Header (metadata) releaseMar 25, 2026-
Map releaseMar 25, 2026-
UpdateMar 25, 2026-
Current statusMar 25, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_65382.png

Downloads & links

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Map

FileDownload / File: emd_65382.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 480 pix.
= 504.96 Å		1.05 Å/pix.
x 480 pix.
= 504.96 Å		1.05 Å/pix.
x 480 pix.
= 504.96 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.052 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 5.0
Minimum - Maximum-0.722902 - 28.404098999999999
Average (Standard dev.)0.034564342 (±0.592636)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 504.96002 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : The erlin1/2 complex

EntireName: The erlin1/2 complex
Components
  • Complex: The erlin1/2 complex
    • Protein or peptide: Erlin-1
    • Protein or peptide: Erlin-2

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Supramolecule #1: The erlin1/2 complex

SupramoleculeName: The erlin1/2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Erlin-1

MacromoleculeName: Erlin-1 / type: protein_or_peptide / ID: 1 / Number of copies: 13 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.46184 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: ARVLVAAVVG LVAVLLYASI HKIEEGHLAV YYRGGALLTS PSGPGYHIML PFITTFRSVQ TTLQTDEVKN VPCGTSGGVM IYIDRIEVV NMLAPYAVFD IVRNYTADYD KTLIFNKIHH ELNQFCSAHT LQEVYIELFD QIDENLKQAL QKDLNLMAPG L TIQAVRVT ...String:
ARVLVAAVVG LVAVLLYASI HKIEEGHLAV YYRGGALLTS PSGPGYHIML PFITTFRSVQ TTLQTDEVKN VPCGTSGGVM IYIDRIEVV NMLAPYAVFD IVRNYTADYD KTLIFNKIHH ELNQFCSAHT LQEVYIELFD QIDENLKQAL QKDLNLMAPG L TIQAVRVT KPKIPEAIRR NFELMEAEKT KLLIAAQKQK VVEKEAETER KKAVIEAEKI AQVAKIRFQQ KVMEKETEKR IS EIEDAAF LAREKAKADA EYYAAHKYAT SNKHKLTPEY LELKKYQAIA SNSKIYFGSN IPNMFVD

UniProtKB: Erlin-1

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Macromolecule #2: Erlin-2

MacromoleculeName: Erlin-2 / type: protein_or_peptide / ID: 2 / Number of copies: 13 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.188473 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: LGAVVAVASS FFCASLFSAV HKIEEGHIGV YYRGGALLTS TSGPGFHLML PFITSYKSVQ TTLQTDEVKN VPCGTSGGVM IYFDRIEVV NFLVPNAVYD IVKNYTADYD KALIFNKIHH ELNQFCSVHT LQEVYIELFD QIDENLKLAL QQDLTSMAPG L VIQAVRVT ...String:
LGAVVAVASS FFCASLFSAV HKIEEGHIGV YYRGGALLTS TSGPGFHLML PFITSYKSVQ TTLQTDEVKN VPCGTSGGVM IYFDRIEVV NFLVPNAVYD IVKNYTADYD KALIFNKIHH ELNQFCSVHT LQEVYIELFD QIDENLKLAL QQDLTSMAPG L VIQAVRVT KPNIPEAIRR NYELMESEKT KLLIAAQKQK VVEKEAETER KKALIEAEKV AQVAEITYGQ KVMEKETEKK IS EIEDAAF LAREKAKADA ECYTAMKIAE ANKLKLTPEY LQLMKYKAIA SNSKMYFGKD IPNMFMD

UniProtKB: Erlin-2

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration10 mg/mL
BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 58.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: DIFFRACTION / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 25074
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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