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- PDB-9i9f: Crystal structure of apoform human eIF4A1 C-terminal domain -

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Basic information

Entry
Database: PDB / ID: 9i9f
TitleCrystal structure of apoform human eIF4A1 C-terminal domain
ComponentsEukaryotic initiation factor 4A-I
KeywordsTRANSLATION / INITIATION FACTOR / DEAD-BOX / HELICASE / ATPASE
Function / homology
Function and homology information


Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / RNA cap binding / eukaryotic translation initiation factor 4F complex / nuclear stress granule / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / cytoplasmic translational initiation / translation factor activity, RNA binding / Deadenylation of mRNA / M-decay: degradation of maternal mRNAs by maternally stored factors / Ribosomal scanning and start codon recognition ...Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / RNA cap binding / eukaryotic translation initiation factor 4F complex / nuclear stress granule / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / cytoplasmic translational initiation / translation factor activity, RNA binding / Deadenylation of mRNA / M-decay: degradation of maternal mRNAs by maternally stored factors / Ribosomal scanning and start codon recognition / Translation initiation complex formation / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / translation initiation factor activity / translational initiation / helicase activity / ISG15 antiviral mechanism / cytoplasmic stress granule / double-stranded RNA binding / RNA helicase activity / RNA helicase / mRNA binding / perinuclear region of cytoplasm / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / RNA binding / extracellular exosome / ATP binding / membrane / plasma membrane / cytoplasm / cytosol
Similarity search - Function
ATP-dependent RNA helicase eIF4A, DEAD-box helicase domain / DEAD-box subfamily ATP-dependent helicases signature. / ATP-dependent RNA helicase DEAD-box, conserved site / RNA helicase, DEAD-box type, Q motif / DEAD-box RNA helicase Q motif profile. / DEAD/DEAH box helicase domain / DEAD/DEAH box helicase / Helicase conserved C-terminal domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. ...ATP-dependent RNA helicase eIF4A, DEAD-box helicase domain / DEAD-box subfamily ATP-dependent helicases signature. / ATP-dependent RNA helicase DEAD-box, conserved site / RNA helicase, DEAD-box type, Q motif / DEAD-box RNA helicase Q motif profile. / DEAD/DEAH box helicase domain / DEAD/DEAH box helicase / Helicase conserved C-terminal domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Eukaryotic initiation factor 4A-I
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.731 Å
AuthorsTurnbull, A.P. / Schmidt, T. / Bushell, M.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Cancer Research UK United Kingdom
CitationJournal: To Be Published
Title: The mechanism of selective eIF4A1-dependent translation
Authors: Schmidt, T. / Turnbull, A.P. / Bushell, M.
History
DepositionFeb 6, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 18, 2026Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Eukaryotic initiation factor 4A-I
B: Eukaryotic initiation factor 4A-I
C: Eukaryotic initiation factor 4A-I


Theoretical massNumber of molelcules
Total (without water)59,5763
Polymers59,5763
Non-polymers00
Water77543
1
A: Eukaryotic initiation factor 4A-I


Theoretical massNumber of molelcules
Total (without water)19,8591
Polymers19,8591
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Eukaryotic initiation factor 4A-I


Theoretical massNumber of molelcules
Total (without water)19,8591
Polymers19,8591
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Eukaryotic initiation factor 4A-I


Theoretical massNumber of molelcules
Total (without water)19,8591
Polymers19,8591
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)84.970, 84.970, 66.420
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number144
Space group name H-MP31
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21A
32A
42A
53A
63A

NCS domain segments:

Beg auth comp-ID: GLU / Beg label comp-ID: GLU / Auth asym-ID: A / Label asym-ID: A

Dom-IDComponent-IDEns-IDEnd auth comp-IDEnd label comp-IDAuth seq-IDLabel seq-ID
111ALAALA240 - 4034 - 167
211ALAALA240 - 4034 - 167
322LEULEU240 - 4004 - 164
422LEULEU240 - 4004 - 164
533LEULEU240 - 4004 - 164
633LEULEU240 - 4004 - 164

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6

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Components

#1: Protein Eukaryotic initiation factor 4A-I / eIF-4A-I / eIF4A-I / ATP-dependent RNA helicase eIF4A-1


Mass: 19858.535 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF4A1, DDX2A, EIF4A / Production host: Escherichia coli (E. coli) / References: UniProt: P60842, RNA helicase
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 43 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.43 Å3/Da / Density % sol: 49.4 % / Description: needle-like
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6
Details: 18.5% (w/v) PEG 8000, 0.2M sodium acetate trihydrate, 0.1M MES, pH 6.0

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Sep 14, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.73→42.49 Å / Num. obs: 14242 / % possible obs: 100 % / Redundancy: 6.4 % / CC1/2: 0.994 / Rrim(I) all: 0.189 / Net I/σ(I): 8.2
Reflection shellResolution: 2.73→2.78 Å / Num. unique obs: 730 / CC1/2: 0.507 / Rrim(I) all: 1.375

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Processing

Software
NameVersionClassification
REFMAC5.8.0425refinement
xia2data reduction
xia2data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.731→40.003 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.881 / SU B: 50.716 / SU ML: 0.445 / Cross valid method: FREE R-VALUE / ESU R Free: 0.431
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2937 674 4.738 %
Rwork0.2287 13550 -
all0.232 --
obs-14224 99.86 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 62.688 Å2
Baniso -1Baniso -2Baniso -3
1-1.372 Å20.686 Å2-0 Å2
2--1.372 Å2-0 Å2
3----4.45 Å2
Refinement stepCycle: LAST / Resolution: 2.731→40.003 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3732 0 0 43 3775
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0123782
X-RAY DIFFRACTIONr_bond_other_d0.0010.0163542
X-RAY DIFFRACTIONr_angle_refined_deg1.4381.8265132
X-RAY DIFFRACTIONr_angle_other_deg0.5231.7638065
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.725482
X-RAY DIFFRACTIONr_dihedral_angle_2_deg5.35528
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.19910608
X-RAY DIFFRACTIONr_dihedral_angle_6_deg14.3410164
X-RAY DIFFRACTIONr_chiral_restr0.070.2621
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.024485
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02859
X-RAY DIFFRACTIONr_nbd_refined0.2410.2812
X-RAY DIFFRACTIONr_symmetry_nbd_other0.2130.23380
X-RAY DIFFRACTIONr_nbtor_refined0.1780.21925
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0850.22152
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1520.292
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.3060.219
X-RAY DIFFRACTIONr_nbd_other0.2020.266
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.2910.26
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.0620.21
X-RAY DIFFRACTIONr_mcbond_it2.9664.031940
X-RAY DIFFRACTIONr_mcbond_other2.9664.031940
X-RAY DIFFRACTIONr_mcangle_it4.8337.2382418
X-RAY DIFFRACTIONr_mcangle_other4.8327.2382419
X-RAY DIFFRACTIONr_scbond_it2.914.081842
X-RAY DIFFRACTIONr_scbond_other2.9094.0811843
X-RAY DIFFRACTIONr_scangle_it4.7837.4572714
X-RAY DIFFRACTIONr_scangle_other4.7827.4572715
X-RAY DIFFRACTIONr_lrange_it7.01537.8224175
X-RAY DIFFRACTIONr_lrange_other7.01437.8254173
X-RAY DIFFRACTIONr_ncsr_local_group_10.1370.054741
X-RAY DIFFRACTIONr_ncsr_local_group_20.1090.054389
X-RAY DIFFRACTIONr_ncsr_local_group_30.090.054477
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.136580.05008
12AX-RAY DIFFRACTIONLocal ncs0.136580.05008
23AX-RAY DIFFRACTIONLocal ncs0.108890.05009
24AX-RAY DIFFRACTIONLocal ncs0.108890.05009
35AX-RAY DIFFRACTIONLocal ncs0.090050.05009
36AX-RAY DIFFRACTIONLocal ncs0.090050.05009
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
2.731-2.8010.407680.4229630.42110320.9150.90999.90310.42
2.801-2.8780.405440.41610100.41610540.9310.9131000.41
2.878-2.9610.375440.3939430.3929870.920.9191000.39
2.961-3.0510.406380.3549270.3569670.9130.92999.79320.342
3.051-3.1510.381580.2878840.2939450.9240.95399.68250.263
3.151-3.2610.307340.2428800.2449160.9380.96499.78170.221
3.261-3.3830.321400.2218070.2258520.9290.9799.41310.2
3.383-3.520.259680.2257730.2288410.9550.9721000.212
3.52-3.6750.347260.2167840.228110.9510.97899.87670.205
3.675-3.8530.193140.1977700.1977840.9770.9811000.189
3.853-4.0590.223240.2076920.2087160.9740.9821000.2
4.059-4.3030.279450.1916510.1966960.9590.9831000.181
4.303-4.5960.247320.1796220.1836540.960.9811000.17
4.596-4.9590.248430.1635680.1696110.9660.9831000.163
4.959-5.4240.289160.2025440.2055600.9360.9771000.193
5.424-6.050.209160.2385040.2375200.9740.9711000.223
6.05-6.960.363260.2274090.2344350.9380.9751000.221
6.96-8.460.241160.2323700.2333860.9750.9731000.231
8.46-11.7050.343150.1732790.182950.9720.98199.6610.188
11.705-40.0030.30670.241700.2431780.9030.96199.43820.261
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
13.9426-0.8219-0.94264.4877-1.35574.5382-0.06710.0333-0.08450.22020.06840.66730.0063-0.4754-0.00130.0144-0.00560.02850.0538-0.01060.1372113.9665-21.6119-7.0429
25.89190.66980.48083.7439-1.73723.1702-0.1909-0.1008-0.4028-0.19590.10850.33670.43-0.23870.08240.1278-0.0396-0.00590.04530.00430.1905117.202314.6685-4.7902
37.0196-0.57892.51480.97711.27595.3528-0.02140.1698-0.30360.0058-0.0163-0.32690.43780.56030.03770.34860.02810.12630.27610.13850.397497.0899-6.263723.8073
Refinement TLS groupSelection: ALL

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