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- EMDB-70263: The Erlin1/2 complex -

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Open data


ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-70263
TitleThe Erlin1/2 complex
Map data
Sample
  • Complex: Complex of 13 Erlin1/2 heterodimers
    • Protein or peptide: Erlin-1
    • Protein or peptide: Erlin-2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
KeywordsSPFH / ER / Erlin1 / Erlin2 / MEMBRANE PROTEIN
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: 3.0 Å
AuthorsGao J / Shao S
Funding support United States, 3 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Aging (NIH/NIA)AG073277 United States
David and Lucile Packard Foundation United States
Richard and Susan Smith Family Foundation United States
CitationJournal: To Be Published
Title: The single particle cryo-EM structure of the Erlin1/2 complex
Authors: Gao J / Shao S
History
DepositionApr 18, 2025-
Header (metadata) releaseOct 22, 2025-
Map releaseOct 22, 2025-
UpdateOct 22, 2025-
Current statusOct 22, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_70263.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 512 pix.
= 424.96 Å
0.83 Å/pix.
x 512 pix.
= 424.96 Å
0.83 Å/pix.
x 512 pix.
= 424.96 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 0.11
Minimum - Maximum-0.6385877 - 1.001736
Average (Standard dev.)0.002133545 (±0.035818852)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 424.96 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_70263_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: #2

Fileemd_70263_additional_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_70263_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_70263_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Complex of 13 Erlin1/2 heterodimers

EntireName: Complex of 13 Erlin1/2 heterodimers
Components
  • Complex: Complex of 13 Erlin1/2 heterodimers
    • Protein or peptide: Erlin-1
    • Protein or peptide: Erlin-2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

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Supramolecule #1: Complex of 13 Erlin1/2 heterodimers

SupramoleculeName: Complex of 13 Erlin1/2 heterodimers / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
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: 42.429402 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KGSGSMTQAR VLVAAVVGLV AVLLYASIHK IEEGHLAVYY RGGALLTSPS GPGYHIMLP FITTFRSVQT TLQTDEVKNV PCGTSGGVMI YIDRIEVVNM LAPYAVFDIV RNYTADYDKT LIFNKIHHEL N QFCSAHTL ...String:
MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KGSGSMTQAR VLVAAVVGLV AVLLYASIHK IEEGHLAVYY RGGALLTSPS GPGYHIMLP FITTFRSVQT TLQTDEVKNV PCGTSGGVMI YIDRIEVVNM LAPYAVFDIV RNYTADYDKT LIFNKIHHEL N QFCSAHTL QEVYIELFDQ IDENLKQALQ KDLNLMAPGL TIQAVRVTKP KIPEAIRRNF ELMEAEKTKL LIAAQKQKVV EK EAETERK KAVIEAEKIA QVAKIRFQQK VMEKETEKRI SEIEDAAFLA REKAKADAEY YAAHKYATSN KHKLTPEYLE LKK YQAIAS NSKIYFGSNI PNMFVDSSCA LKYSDIRTGR ESSLPSKEAL EPSGENVIQN KESTG

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: 37.884473 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAQLGAVVAV ASSFFCASLF SAVHKIEEGH IGVYYRGGAL LTSTSGPGFH LMLPFITSYK SVQTTLQTDE VKNVPCGTSG GVMIYFDRI EVVNFLVPNA VYDIVKNYTA DYDKALIFNK IHHELNQFCS VHTLQEVYIE LFDQIDENLK LALQQDLTSM A PGLVIQAV ...String:
MAQLGAVVAV ASSFFCASLF SAVHKIEEGH IGVYYRGGAL LTSTSGPGFH LMLPFITSYK SVQTTLQTDE VKNVPCGTSG GVMIYFDRI EVVNFLVPNA VYDIVKNYTA DYDKALIFNK IHHELNQFCS VHTLQEVYIE LFDQIDENLK LALQQDLTSM A PGLVIQAV RVTKPNIPEA IRRNYELMES EKTKLLIAAQ KQKVVEKEAE TERKKALIEA EKVAQVAEIT YGQKVMEKET EK KISEIED AAFLAREKAK ADAECYTAMK IAEANKLKLT PEYLQLMKYK AIASNSKIYF GKDIPNMFMD SAGSVSKQFE GLA DKLSFG LEDEPLETAT KEN

UniProtKB: Erlin-2

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Macromolecule #3: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 3 / Number of copies: 26 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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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

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 52.32 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 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: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 95469
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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