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- EMDB-72462: Eukaryotic translation initiation factor 2-B in its apo form (act... -

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Basic information

Entry
Database: EMDB / ID: EMD-72462
TitleEukaryotic translation initiation factor 2-B in its apo form (active-state) (CASP target)
Map data
Sample
  • Complex: Eukaryotic translation initiation factor 2B
    • Protein or peptide: Translation initiation factor eIF2B subunit epsilon
    • Protein or peptide: Translation initiation factor eIF2B subunit beta
    • Protein or peptide: Translation initiation factor eIF2B subunit delta
    • Protein or peptide: Translation initiation factor eIF2B subunit delta
    • Protein or peptide: Translation initiation factor eIF-2B subunit alpha
    • Protein or peptide: Translation initiation factor eIF2B subunit gamma
  • Ligand: CHLORIDE ION
  • Ligand: IMIDAZOLE
  • Ligand: ZINC ION
KeywordsGuanine nucleotide exchange factor / GEF / translation / initiation
Function / homology
Function and homology information


eukaryotic translation initiation factor 2B complex / Recycling of eIF2:GDP / astrocyte development / astrocyte differentiation / oligodendrocyte development / regulation of translational initiation / cytoplasmic translational initiation / ovarian follicle development / response to glucose / positive regulation of translational initiation ...eukaryotic translation initiation factor 2B complex / Recycling of eIF2:GDP / astrocyte development / astrocyte differentiation / oligodendrocyte development / regulation of translational initiation / cytoplasmic translational initiation / ovarian follicle development / response to glucose / positive regulation of translational initiation / myelination / translation initiation factor activity / translation initiation factor binding / guanyl-nucleotide exchange factor activity / response to endoplasmic reticulum stress / hippocampus development / central nervous system development / translational initiation / response to peptide hormone / T cell receptor signaling pathway / regulation of translation / response to heat / positive regulation of apoptotic process / GTP binding / ATP binding / membrane / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Translation initiation factor eIF-2B subunit alpha, N-terminal / Translation initiation factor eIF-2B subunit epsilon, N-terminal / Translation initiation factor eIF-2B subunit epsilon, W2 domain / : / : / : / : / : / EIF2B subunit epsilon LbH domain / Initiation factor 2B-related ...Translation initiation factor eIF-2B subunit alpha, N-terminal / Translation initiation factor eIF-2B subunit epsilon, N-terminal / Translation initiation factor eIF-2B subunit epsilon, W2 domain / : / : / : / : / : / EIF2B subunit epsilon LbH domain / Initiation factor 2B-related / Initiation factor 2B-like, C-terminal / Initiation factor 2 subunit family / eIF4-gamma/eIF5/eIF2-epsilon / Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5 / W2 domain / W2 domain profile. / Nucleotidyl transferase domain / Nucleotidyl transferase / NagB/RpiA transferase-like / Trimeric LpxA-like superfamily / Nucleotide-diphospho-sugar transferases / Armadillo-type fold
Similarity search - Domain/homology
Translation initiation factor eIF2B subunit beta / Translation initiation factor eIF2B subunit epsilon / Translation initiation factor eIF2B subunit alpha / Translation initiation factor eIF2B subunit gamma / Translation initiation factor eIF2B subunit delta
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsDalwadi U / Croll T / Subramanian A / Lee DJ / Arthur C / Walter P / Frost A
Funding support United States, 1 items
OrganizationGrant numberCountry
Other private United States
CitationJournal: Nat Chem Biol / Year: 2026
Title: Allosteric disordering of eIF2B regulates the integrated stress response.
Authors: Udit Dalwadi / Advait Subramanian / Aniliese Deal / Julia E Conrad / Tamara Nadjsombati / Meera Venkatesh / Morgane Boone / Pascal F Egea / Lingjie He / Nimit Jain / D John Lee / Yuwei Liu / ...Authors: Udit Dalwadi / Advait Subramanian / Aniliese Deal / Julia E Conrad / Tamara Nadjsombati / Meera Venkatesh / Morgane Boone / Pascal F Egea / Lingjie He / Nimit Jain / D John Lee / Yuwei Liu / Lucas C Reineke / Kazuki Saito / Nathaniel Talledge / Hannah Toutkoushian / Maxence Le Vasseur / Francesca Zappa / Raoul J de Groot / Diego Acosta-Alvear / Christopher P Arthur / Jodi Nunnari / Susan Marqusee / Rosalie E Lawrence / Mauro Costa-Mattioli / James J Crawford / Frank J M van Kuppeveld / Tristan I Croll / Peter Walter / Adam Frost /
Abstract: The ternary complex, composed of eIF2, GTP and initiator methionyl-tRNA, delivers the first amino acid to the ribosome to initiate protein synthesis. Eukaryotic initiation factor 2B (eIF2B) catalyzes ...The ternary complex, composed of eIF2, GTP and initiator methionyl-tRNA, delivers the first amino acid to the ribosome to initiate protein synthesis. Eukaryotic initiation factor 2B (eIF2B) catalyzes GDP to GTP exchange on eIF2, thereby setting the ternary complex level. Stress-induced phosphorylation converts eIF2 from the substrate of eIF2B into an inhibitor (eIF2-P). This conversion reduces ternary complex levels and induces the integrated stress response (ISR). Here we chart an allosteric axis running through eIF2B, revealing the importance of an α-helix in its β-subunit, the 'latch-helix', that hooks onto the α-subunit to induce eIF2B activity. eIF2-P binding promotes latch-helix unhooking, opening eIF2B, which inhibits its activity. Convergently evolved viral proteins stabilize this latch-helix-binding active state of eIF2B. Using these insights, we generated ISR-activating compounds that stabilize eIF2B in its inhibited, unlatched state. Our study thus highlights how long-range eIF2B allostery can be pharmacologically manipulated to sustain or attenuate the ISR.
History
DepositionSep 2, 2025-
Header (metadata) releaseJun 24, 2026-
Map releaseJun 24, 2026-
UpdateJul 15, 2026-
Current statusJul 15, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_72462.png

Downloads & links

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Map

FileDownload / File: emd_72462.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.14 Å/pix.
x 400 pix.
= 457.52 Å		1.14 Å/pix.
x 400 pix.
= 457.52 Å		1.14 Å/pix.
x 400 pix.
= 457.52 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1438 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.05
Minimum - Maximum-1.7530653 - 4.360888
Average (Standard dev.)-0.00046545174 (±0.111110136)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 457.52002 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_72462_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_72462_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Eukaryotic translation initiation factor 2B

EntireName: Eukaryotic translation initiation factor 2B
Components
  • Complex: Eukaryotic translation initiation factor 2B
    • Protein or peptide: Translation initiation factor eIF2B subunit epsilon
    • Protein or peptide: Translation initiation factor eIF2B subunit beta
    • Protein or peptide: Translation initiation factor eIF2B subunit delta
    • Protein or peptide: Translation initiation factor eIF2B subunit delta
    • Protein or peptide: Translation initiation factor eIF-2B subunit alpha
    • Protein or peptide: Translation initiation factor eIF2B subunit gamma
  • Ligand: CHLORIDE ION
  • Ligand: IMIDAZOLE
  • Ligand: ZINC ION

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Supramolecule #1: Eukaryotic translation initiation factor 2B

SupramoleculeName: Eukaryotic translation initiation factor 2B / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 521.758 KDa

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Macromolecule #1: Translation initiation factor eIF2B subunit epsilon

MacromoleculeName: Translation initiation factor eIF2B subunit epsilon / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 51.385105 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: PPPPLQAVLV ADSFDRRFFP ISKDQPRVLL PLANVALIDY TLEFLTATGV QETFVFCCWK AAQIKEHLLK SKWCRPTSLN VVRIITSEL YRSLGDVLRD VDAKALVRSD FLLVYGDVIS NINITRALEE HRLRRKLEKN VSVMTMIFKE SSPSHPTRCH E DNVVVAVD ...String:
PPPPLQAVLV ADSFDRRFFP ISKDQPRVLL PLANVALIDY TLEFLTATGV QETFVFCCWK AAQIKEHLLK SKWCRPTSLN VVRIITSEL YRSLGDVLRD VDAKALVRSD FLLVYGDVIS NINITRALEE HRLRRKLEKN VSVMTMIFKE SSPSHPTRCH E DNVVVAVD STTNRVLHFQ KTQGLRRFAF PLSLFQGSSD GVEVRYDLLD CHISICSPQV AQLFTDNFDY QTRDDFVRGL LV NEEILGN QIHMHVTAKE YGARVSNLHM YSAVCADVIR RWVYPLTPEA NFTDSTTQSC THSRHNIYRG PEVSLGHGSI LEE NVLLGS GTVIGSNCFI TNSVIGPGCH IGDNVVLDQT YLWQGVRVAA GAQIHQSLLC DNAEVKERVT LKPRSVLTSQ VVVG PNITL PEGSVISLHP PDAEEDEDDG EFSDDSGADQ EKDKVKMKGY NPAEVGAAGK GYLWKA

UniProtKB: Translation initiation factor eIF2B subunit epsilon

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Macromolecule #2: Translation initiation factor eIF2B subunit beta

MacromoleculeName: Translation initiation factor eIF2B subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 38.395773 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GSELSERIES FVETLKRGGG PRSSEEMARE TLGLLRQIIT DHRWSNAGEL MELIRREGRR MTAAQPSETT VGNMVRRVLK IIREEYGRL HGRSDESDQQ ESLHKLLTSG GLNEDFSFHY AQLQSNIIEA INELLVELEG TMENIAAQAL EHIHSNEVIM T IGFSRTVE ...String:
GSELSERIES FVETLKRGGG PRSSEEMARE TLGLLRQIIT DHRWSNAGEL MELIRREGRR MTAAQPSETT VGNMVRRVLK IIREEYGRL HGRSDESDQQ ESLHKLLTSG GLNEDFSFHY AQLQSNIIEA INELLVELEG TMENIAAQAL EHIHSNEVIM T IGFSRTVE AFLKEAARKR KFHVIVAECA PFCQGHEMAV NLSKAGIETT VMTDAAIFAV MSRVNKVIIG TKTILANGAL RA VTGTHTL ALAAKHHSTP LIVCAPMFKL SPQFPNEEDS FHKFVAPEEV LPFTEGDILE KVSVHCPVFD YVPPELITLF ISN IGGNAP SYIYRLMSEL YHPDDHVL

UniProtKB: Translation initiation factor eIF2B subunit beta

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Macromolecule #3: Translation initiation factor eIF2B subunit delta

MacromoleculeName: Translation initiation factor eIF2B subunit delta / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.617582 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: QVPTRKDYGS KVSLFSHLPQ YSRQNSLTQF MSIPSSVIHP AMVRLGLQYS QGLVSGSNAR CIALLRALQQ VIQDYTTPPN EELSRDLVN KLKPYMSFLT QCRPLSASMH NAIKFLNKEI TSVGSSKREE EAKSELRAAI DRYVQEKIVL AAQAISRFAY Q KISNGDVI ...String:
QVPTRKDYGS KVSLFSHLPQ YSRQNSLTQF MSIPSSVIHP AMVRLGLQYS QGLVSGSNAR CIALLRALQQ VIQDYTTPPN EELSRDLVN KLKPYMSFLT QCRPLSASMH NAIKFLNKEI TSVGSSKREE EAKSELRAAI DRYVQEKIVL AAQAISRFAY Q KISNGDVI LVYGCSSLVS RILQEAWTEG RRFRVVVVDS RPWLEGRHTL RSLVHAGVPA SYLLIPAASY VLPEVSKVLL GA HALLANG SVMSRVGTAQ LALVARAHNV PVLVCCETYK FCERVQTDAF VSNELDDPDD LQCKRGEHVA LANWQNHASL RLL NLVYDV TPPELVDLVI TELGMIPCSS VPVVLRVKSS D

UniProtKB: Translation initiation factor eIF2B subunit delta

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Macromolecule #4: Translation initiation factor eIF2B subunit delta

MacromoleculeName: Translation initiation factor eIF2B subunit delta / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.489453 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: VPTRKDYGSK VSLFSHLPQY SRQNSLTQFM SIPSSVIHPA MVRLGLQYSQ GLVSGSNARC IALLRALQQV IQDYTTPPNE ELSRDLVNK LKPYMSFLTQ CRPLSASMHN AIKFLNKEIT SVGSSKREEE AKSELRAAID RYVQEKIVLA AQAISRFAYQ K ISNGDVIL ...String:
VPTRKDYGSK VSLFSHLPQY SRQNSLTQFM SIPSSVIHPA MVRLGLQYSQ GLVSGSNARC IALLRALQQV IQDYTTPPNE ELSRDLVNK LKPYMSFLTQ CRPLSASMHN AIKFLNKEIT SVGSSKREEE AKSELRAAID RYVQEKIVLA AQAISRFAYQ K ISNGDVIL VYGCSSLVSR ILQEAWTEGR RFRVVVVDSR PWLEGRHTLR SLVHAGVPAS YLLIPAASYV LPEVSKVLLG AH ALLANGS VMSRVGTAQL ALVARAHNVP VLVCCETYKF CERVQTDAFV SNELDDPDDL QCKRGEHVAL ANWQNHASLR LLN LVYDVT PPELVDLVIT ELGMIPCSSV PVVLRVKSSD

UniProtKB: Translation initiation factor eIF2B subunit delta

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Macromolecule #5: Translation initiation factor eIF-2B subunit alpha

MacromoleculeName: Translation initiation factor eIF-2B subunit alpha / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 33.754148 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT SAIETLCGVD SSVAVSSGGE LFLRFISLAS LEYSDYSKC KKIMIERGEL FLRRISLSRN KIADLCHTFI KDGATILTHA YSRVVLRVLE AAVAAKKRFS VYVTESQPDL S GKKMAKAL ...String:
MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT SAIETLCGVD SSVAVSSGGE LFLRFISLAS LEYSDYSKC KKIMIERGEL FLRRISLSRN KIADLCHTFI KDGATILTHA YSRVVLRVLE AAVAAKKRFS VYVTESQPDL S GKKMAKAL CHLNVPVTVV LDAAVGYIME KADLVIVGAE GVVENGGIIN KIGTNQMAVC AKAQNKPFYV VAESFKFVRL FP LNQQDVP DKFKYKADTL KVAQTGQDLK EEHPWVDYTA PSLITLLFTD LGVLTPSAVS DELIKLYL

UniProtKB: Translation initiation factor eIF2B subunit alpha

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Macromolecule #6: Translation initiation factor eIF2B subunit gamma

MacromoleculeName: Translation initiation factor eIF2B subunit gamma / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 49.304109 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MEFQAVVMAV GGGSRMTDLT SSIPKPLLPV GNKPLIWYPL NLLERVGFEE VIVVTTRDVQ KALCAEFKMK MKPDIVCIPD DADMGTADS LRYIYPKLKT DVLVLSCDLI TDVALHEVVD LFRAYDASLA MLMRKGQDSI EPVPGQKGKK KAVEQRDFIG V DSTGKRLL ...String:
MEFQAVVMAV GGGSRMTDLT SSIPKPLLPV GNKPLIWYPL NLLERVGFEE VIVVTTRDVQ KALCAEFKMK MKPDIVCIPD DADMGTADS LRYIYPKLKT DVLVLSCDLI TDVALHEVVD LFRAYDASLA MLMRKGQDSI EPVPGQKGKK KAVEQRDFIG V DSTGKRLL FMANEADLDE ELVIKGSILQ KHPRIRFHTG LVDAHLYCLK KYIVDFLMEN GSITSIRSEL IPYLVRKQFS SA SSQQGQE EKEEDLKKKE LKSLDIYSFI KEANTLNLAP YDACWNACRG DRWEDLSRSQ VRCYVHIMKE GLCSRVSTLG LYM EANRQV PKLLSALCPE EPPVHSSAQI VSKHLVGVDS LIGPETQIGE KSSIKRSVIG SSCLIKDRVT ITNCLLMNSV TVEE GSNIQ GSVICNNAVI EKGADIKDCL IGSGQRIEAK AKRVNEVI

UniProtKB: Translation initiation factor eIF2B subunit gamma

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Macromolecule #7: CHLORIDE ION

MacromoleculeName: CHLORIDE ION / type: ligand / ID: 7 / Number of copies: 11 / Formula: CL
Molecular weightTheoretical: 35.453 Da

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Macromolecule #8: IMIDAZOLE

MacromoleculeName: IMIDAZOLE / type: ligand / ID: 8 / Number of copies: 2 / Formula: IMD
Molecular weightTheoretical: 69.085 Da
Chemical component information

ChemComp-IMD:
IMIDAZOLE

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Macromolecule #9: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 9 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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

Concentration6 mg/mL
BufferpH: 7.4
Component:
ConcentrationFormulaName
20.0 mMHEPES2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid or 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acid
200.0 mMKClPotassium Chloride
5.0 mMMgCl2Magnesium Chloride
1.0 mMTCEPtris(2-carboxyethyl)phosphine

Details: 20 mM HEPES KOH pH 7.4, 200 mM KCl, 5 mM MgCl2, 1 mM TCEP
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 25 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.00045000000000000004 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: LEICA EM GP

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Electron microscopy

MicroscopeTFS GLACIOS
Specialist opticsEnergy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number grids imaged: 2 / Number real images: 18826 / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 130000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN

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Image processing

Particle selectionNumber selected: 890578
CTF correctionSoftware - Name: cryoSPARC (ver. 4.2.1) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.2.1) / Number images used: 60012
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.2.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.2.1)
Final 3D classificationNumber classes: 10 / Avg.num./class: 56900 / Software - Name: cryoSPARC (ver. 4.2.1)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

7l7g


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementProtocol: AB INITIO MODEL
Output model

PDB-9y3p:
Eukaryotic translation initiation factor 2-B in its apo form (active-state)

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