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- PDB-5abx: Complex of C. elegans eIF4E-3 with the 4E-binding protein Mextli ... -

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Basic information

Entry
Database: PDB / ID: 5abx
TitleComplex of C. elegans eIF4E-3 with the 4E-binding protein Mextli and cap analog
Components
  • 4E-BINDING PROTEIN MEXTLI
  • EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-3
KeywordsTRANSLATION / GENE REGULATION / CAP BINDING PROTEIN / 4E BINDING PROTEIN
Function / homology
Function and homology information


translation initiation complex / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / regulation of formation of translation initiation ternary complex / ISG15 antiviral mechanism / L13a-mediated translational silencing of Ceruloplasmin expression / Translation initiation complex formation / Ribosomal scanning and start codon recognition / 21U-RNA metabolic process / RNA cap binding complex / piRNA processing ...translation initiation complex / Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S / regulation of formation of translation initiation ternary complex / ISG15 antiviral mechanism / L13a-mediated translational silencing of Ceruloplasmin expression / Translation initiation complex formation / Ribosomal scanning and start codon recognition / 21U-RNA metabolic process / RNA cap binding complex / piRNA processing / eukaryotic initiation factor 4E binding / eukaryotic translation initiation factor 4F complex / RNA 7-methylguanosine cap binding / embryo development ending in birth or egg hatching / translation initiation factor activity / positive regulation of translation / translational initiation / perinuclear region of cytoplasm / RNA binding / cytoplasm
Similarity search - Function
Eukaryotic translation initiation factor 4E-binding protein Mextli / RNA Cap, Translation Initiation Factor Eif4e / RNA Cap, Translation Initiation Factor Eif4e / Eukaryotic translation initiation factor 4E (eIF-4E), conserved site / Eukaryotic initiation factor 4E signature. / Translation Initiation factor eIF- 4e / Eukaryotic initiation factor 4E / Translation Initiation factor eIF- 4e-like / KH domain / K Homology domain, type 1 ...Eukaryotic translation initiation factor 4E-binding protein Mextli / RNA Cap, Translation Initiation Factor Eif4e / RNA Cap, Translation Initiation Factor Eif4e / Eukaryotic translation initiation factor 4E (eIF-4E), conserved site / Eukaryotic initiation factor 4E signature. / Translation Initiation factor eIF- 4e / Eukaryotic initiation factor 4E / Translation Initiation factor eIF- 4e-like / KH domain / K Homology domain, type 1 / Type-1 KH domain profile. / K Homology domain, type 1 superfamily / K Homology domain / K homology RNA-binding domain / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
7-METHYL-GUANOSINE-5'-TRIPHOSPHATE / Eukaryotic translation initiation factor 4E-3 / Eukaryotic translation initiation factor 4E-binding protein Mextli homolog
Similarity search - Component
Biological speciesCAENORHABDITIS ELEGANS (invertebrata)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.66 Å
AuthorsPeter, D. / Weichenrieder, O.
CitationJournal: Genes Dev. / Year: 2015
Title: Mextli Proteins Use Both Canonical Bipartite and Novel Tripartite Binding Modes to Form Eif4E Complexes that Display Differential Sensitivity to 4E-BP Regulation
Authors: Peter, D. / Weber, R. / Koene, C. / Chung, M.-Y. / Ebertsch, L. / Truffault, V. / Weichenrieder, O. / Igreja, C. / Izaurralde, E.
History
DepositionAug 9, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 2, 2015Provider: repository / Type: Initial release
Revision 1.1Sep 23, 2015Group: Database references
Revision 1.2May 8, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-3
B: 4E-BINDING PROTEIN MEXTLI
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9538
Polymers27,1182
Non-polymers8356
Water2,468137
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3150 Å2
ΔGint-14 kcal/mol
Surface area13340 Å2
MethodPQS
Unit cell
Length a, b, c (Å)71.040, 71.040, 85.280
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Components on special symmetry positions
IDModelComponents
11A-1218-

ZN

21B-1509-

ZN

31A-2051-

HOH

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Components

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Protein / Protein/peptide , 2 types, 2 molecules AB

#1: Protein EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-3 / EIF-4E-3 / EIF4E-3 / EIF-4F 25 KDA SUBUNIT / MRNA CAP-BINDING PROTEIN / EUKARYOTIC TRANSLATION ...EIF-4E-3 / EIF4E-3 / EIF-4F 25 KDA SUBUNIT / MRNA CAP-BINDING PROTEIN / EUKARYOTIC TRANSLATION INITIATION FACTOR 4E


Mass: 22377.488 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 30-215
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) CAENORHABDITIS ELEGANS (invertebrata) / Plasmid: PETMCN (PNYC) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): STAR / References: UniProt: O61955
#2: Protein/peptide 4E-BINDING PROTEIN MEXTLI


Mass: 4740.511 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 471-507
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) CAENORHABDITIS ELEGANS (invertebrata) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): STAR / References: UniProt: Q9XW13

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Non-polymers , 4 types, 143 molecules

#3: Chemical ChemComp-MGP / 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE


Mass: 538.215 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H19N5O14P3
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 137 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsTHE FIRST FOUR RESIDUES OF CHAIN A REMAIN FROM THE EXPRESSION TAG. THE FIRST FOUR RESIDUES OF CHAIN ...THE FIRST FOUR RESIDUES OF CHAIN A REMAIN FROM THE EXPRESSION TAG. THE FIRST FOUR RESIDUES OF CHAIN B REMAIN FROM THE EXPRESSION TAG.

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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: 2.17 Å3/Da / Density % sol: 43.5 % / Description: NONE
Crystal growpH: 5
Details: 0.1M SODIUM ACETATE, PH=5.0, 0.01M ZNCL2, 18% PEG6000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1.00001
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 27, 2015 / Details: DYNAMICALLY BENDABLE MIRRORS
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00001 Å / Relative weight: 1
ReflectionResolution: 1.66→43.3 Å / Num. obs: 26447 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 13.1 % / Biso Wilson estimate: 25.3 Å2 / Rsym value: 0.06 / Net I/σ(I): 24.5
Reflection shellResolution: 1.66→1.7 Å / Redundancy: 12 % / Mean I/σ(I) obs: 2 / Rsym value: 1.27 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.9_1692)refinement
XDSdata reduction
XSCALEdata scaling
SHELXphasing
RefinementMethod to determine structure: SAD
Starting model: NONE

Resolution: 1.66→43.282 Å / SU ML: 0.17 / σ(F): 1.36 / Phase error: 20.75 / Stereochemistry target values: ML
Details: HYDROGENS WERE REFINED IN THE RIDING POSITIONS. THE FOLLOWING RESIDUES WERE MODELED AS DOUBLE CONFORMATIONS. CHAIN A, RESIDUE 135. CHAIN B, RESIDUES 479, 480, 500. THE FOLLOWING RESIDUES ARE ...Details: HYDROGENS WERE REFINED IN THE RIDING POSITIONS. THE FOLLOWING RESIDUES WERE MODELED AS DOUBLE CONFORMATIONS. CHAIN A, RESIDUE 135. CHAIN B, RESIDUES 479, 480, 500. THE FOLLOWING RESIDUES ARE DISORDERED. CHAIN A, RESIDUES 114 TO 120, 204 TO 209. CHAIN B, RESIDUES 484 TO 486. RESTRAINTS FOR THE MGP LIGAND WERE GENERATED WITH GRADE.
RfactorNum. reflection% reflection
Rfree0.1938 2479 5 %
Rwork0.1733 --
obs0.1743 26447 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 31.6 Å2
Refinement stepCycle: LAST / Resolution: 1.66→43.282 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1741 0 38 137 1916
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0061837
X-RAY DIFFRACTIONf_angle_d0.9682506
X-RAY DIFFRACTIONf_dihedral_angle_d12.455694
X-RAY DIFFRACTIONf_chiral_restr0.038270
X-RAY DIFFRACTIONf_plane_restr0.004329
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.66-1.69190.28961370.24882653X-RAY DIFFRACTION100
1.6919-1.72650.28151350.24642565X-RAY DIFFRACTION100
1.7265-1.7640.28751390.23172616X-RAY DIFFRACTION100
1.764-1.80510.26461340.23152592X-RAY DIFFRACTION100
1.8051-1.85020.23211420.21542603X-RAY DIFFRACTION100
1.8502-1.90020.26571390.2092553X-RAY DIFFRACTION100
1.9002-1.95610.20461380.19142625X-RAY DIFFRACTION100
1.9561-2.01930.21781400.18552599X-RAY DIFFRACTION100
2.0193-2.09140.22271400.1862631X-RAY DIFFRACTION100
2.0914-2.17520.23041340.17372567X-RAY DIFFRACTION100
2.1752-2.27420.21791360.17212604X-RAY DIFFRACTION100
2.2742-2.39410.1891380.16412604X-RAY DIFFRACTION100
2.3941-2.5440.19071340.16132596X-RAY DIFFRACTION100
2.544-2.74040.19491300.17492613X-RAY DIFFRACTION100
2.7404-3.01620.16691390.17022584X-RAY DIFFRACTION100
3.0162-3.45250.21161430.17342600X-RAY DIFFRACTION100
3.4525-4.34910.15321370.14692592X-RAY DIFFRACTION100
4.3491-43.2970.17351440.16922606X-RAY DIFFRACTION100

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