[English] 日本語
Yorodumi
- PDB-8uh1: Crystal structure of T. brucei EIF4E6 in complex with EIF4G5 peptide -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8uh1
TitleCrystal structure of T. brucei EIF4E6 in complex with EIF4G5 peptide
Components
  • Eukaryotic translation initiation factor 4E type 6
  • MIF4G domain-containing protein
KeywordsTRANSLATION / Translation initiation factor / eIF4E family / EIF4E6 / EIF4G5
Function / homology
Function and homology information


RNA cap 4 binding / motile cilium assembly / eukaryotic translation initiation factor 4F complex / RNA 7-methylguanosine cap binding / post-transcriptional regulation of gene expression / translation initiation factor activity / cell motility / mRNA binding / cytoplasm
Similarity search - Function
Initiation factor 4G / Translation Initiation factor eIF- 4e-like / MIF4G domain / Middle domain of eukaryotic initiation factor 4G (eIF4G) / MIF4G-like, type 3 / Armadillo-type fold
Similarity search - Domain/homology
Eukaryotic translation initiation factor 4E type 6 / MIF4G domain-containing protein
Similarity search - Component
Biological speciesTrypanosoma brucei (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.898 Å
AuthorsGuimaraes, B.G. / Penteado, R.F.
Funding support France, Brazil, 3items
OrganizationGrant numberCountry
Pasteur InstituteACIP grant PTR 190 France
Brazilian National Council for Scientific and Technological Development (CNPq)442323/2019-0 Brazil
Brazilian National Council for Scientific and Technological Development (CNPq)305095/2021-8 Brazil
CitationJournal: Sci Rep / Year: 2024
Title: Structural analysis of the Trypanosoma brucei EIF4E6/EIF4G5 complex reveals details of the interaction between unusual eIF4F subunits.
Authors: Ferras Penteado, R. / Santana da Silva, R. / Nascimento Moura, D.M. / Barbosa de Lima, G. / Muniz Malvezzi, A. / Tamara da Silva Monteiro, T. / Cavalcanti Xavier, C. / Vichier-Guerre, S. / ...Authors: Ferras Penteado, R. / Santana da Silva, R. / Nascimento Moura, D.M. / Barbosa de Lima, G. / Muniz Malvezzi, A. / Tamara da Silva Monteiro, T. / Cavalcanti Xavier, C. / Vichier-Guerre, S. / Dugue, L. / Pochet, S. / Tonin Zanchin, N.I. / de Souza Reis, C.R. / Pompilio de Melo Neto, O. / Gomes Guimaraes, B.
History
DepositionOct 6, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 28, 2024Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Eukaryotic translation initiation factor 4E type 6
B: MIF4G domain-containing protein


Theoretical massNumber of molelcules
Total (without water)26,5702
Polymers26,5702
Non-polymers00
Water2,162120
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2690 Å2
ΔGint-25 kcal/mol
Surface area9360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)65.503, 131.185, 59.659
Angle α, β, γ (deg.)90, 90, 90
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11A-284-

HOH

-
Components

#1: Protein Eukaryotic translation initiation factor 4E type 6


Mass: 21800.840 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Trypanosoma brucei (eukaryote) / Production host: Escherichia coli (E. coli) / References: UniProt: Q57V43
#2: Protein/peptide MIF4G domain-containing protein


Mass: 4769.366 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Trypanosoma brucei (eukaryote) / Production host: Escherichia coli (E. coli) / References: UniProt: Q57VY5
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 120 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.41 Å3/Da / Density % sol: 49 %
Crystal growTemperature: 291 K / Method: vapor diffusion
Details: Complex at 12 mg/mL in 20 mM Tris-HCl, 150 mM NaCl, 2 mM DTT, pH 8.0 (pre-incubated with cap-4) with crystallization buffer containing 33% Precipitant Mix 4, 0.09 M NPS, 0.12 M Ethylene ...Details: Complex at 12 mg/mL in 20 mM Tris-HCl, 150 mM NaCl, 2 mM DTT, pH 8.0 (pre-incubated with cap-4) with crystallization buffer containing 33% Precipitant Mix 4, 0.09 M NPS, 0.12 M Ethylene glycols, 0.1 M Buffer System 3 (pH 8.5), from Morpheus Screen mixes

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 2 / Wavelength: 0.978565 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 11, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.978565 Å / Relative weight: 1
ReflectionResolution: 1.9→44 Å / Num. obs: 16430 / % possible obs: 95.1 % / Redundancy: 13.3 % / CC1/2: 0.99 / Net I/σ(I): 13.2
Reflection shellResolution: 1.9→1.97 Å / Num. unique obs: 822 / CC1/2: 0.54

-
Processing

Software
NameVersionClassification
BUSTER2.10.4refinement
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.898→44 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.942 / SU R Cruickshank DPI: 0.164 / Cross valid method: THROUGHOUT / SU R Blow DPI: 0.171 / SU Rfree Blow DPI: 0.148 / SU Rfree Cruickshank DPI: 0.145
RfactorNum. reflection% reflectionSelection details
Rfree0.2219 1102 -RANDOM
Rwork0.1923 ---
obs0.1942 16430 79.2 %-
Displacement parametersBiso mean: 37.26 Å2
Baniso -1Baniso -2Baniso -3
1-1.1333 Å20 Å20 Å2
2---0.1485 Å20 Å2
3----0.9848 Å2
Refine analyzeLuzzati coordinate error obs: 0.24 Å
Refinement stepCycle: LAST / Resolution: 1.898→44 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1557 0 0 120 1677
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0081605HARMONIC2
X-RAY DIFFRACTIONt_angle_deg0.92193HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d524SINUSOIDAL2
X-RAY DIFFRACTIONt_gen_planes264HARMONIC5
X-RAY DIFFRACTIONt_it1605HARMONIC10
X-RAY DIFFRACTIONt_chiral_improper_torsion210SEMIHARMONIC5
X-RAY DIFFRACTIONt_ideal_dist_contact1290SEMIHARMONIC4
X-RAY DIFFRACTIONt_omega_torsion3.39
X-RAY DIFFRACTIONt_other_torsion14.67
LS refinement shellResolution: 1.9→1.93 Å
RfactorNum. reflection% reflection
Rfree0.321 20 -
Rwork0.2467 --
obs0.2506 329 31.55 %
Refinement TLS params.

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)
12.4480.9528-0.86843.6043-1.67467.7540.1644-0.00730.6551-0.0073-0.02380.43490.65510.4349-0.1406-0.03020.0377-0.0444-0.0569-0.0328-0.0902-1.2484-16.95291.9718
21.52270.5643-0.29595.3058-0.6715.12840.0802-0.34680.6547-0.3468-0.0004-0.5410.6547-0.541-0.0798-0.021-0.0737-0.0449-0.0581-0.0138-0.093-13.6698-17.4406-3.5908
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{ B|* }B79 - 118
2X-RAY DIFFRACTION2{ A|* }A7 - 178

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more