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- PDB-1q8k: Solution structure of alpha subunit of human eIF2 -

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Basic information

Entry
Database: PDB / ID: 1q8k
TitleSolution structure of alpha subunit of human eIF2
ComponentsEukaryotic translation initiation factor 2 subunit 1
KeywordsTRANSLATION / Translation Initiation / Eukaryotic translation initiation factor 2
Function / homology
Function and homology information


regulation of translation in response to endoplasmic reticulum stress / translation initiation ternary complex / glial limiting end-foot / response to kainic acid / response to manganese-induced endoplasmic reticulum stress / positive regulation of type B pancreatic cell apoptotic process / Response of EIF2AK1 (HRI) to heme deficiency / negative regulation of translational initiation in response to stress / Recycling of eIF2:GDP / PERK-mediated unfolded protein response ...regulation of translation in response to endoplasmic reticulum stress / translation initiation ternary complex / glial limiting end-foot / response to kainic acid / response to manganese-induced endoplasmic reticulum stress / positive regulation of type B pancreatic cell apoptotic process / Response of EIF2AK1 (HRI) to heme deficiency / negative regulation of translational initiation in response to stress / Recycling of eIF2:GDP / PERK-mediated unfolded protein response / eukaryotic translation initiation factor 2 complex / PERK regulates gene expression / regulation of translational initiation in response to stress / : / eukaryotic 48S preinitiation complex / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / Translation initiation complex formation / Response of EIF2AK4 (GCN2) to amino acid deficiency / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / stress granule assembly / translational initiation / cellular response to amino acid starvation / translation initiation factor activity / response to endoplasmic reticulum stress / PKR-mediated signaling / ABC-family proteins mediated transport / cytoplasmic stress granule / cellular response to UV / ribosome binding / cellular response to oxidative stress / cellular response to heat / synapse / RNA binding / extracellular exosome / membrane / nucleus / cytosol
Similarity search - Function
EIF_2_alpha / Translation initiation factor 2; subunit 1; domain 2 / IF2a, S1-like domain / Translation initiation factor 2, alpha subunit / Translation initiation factor 2, alpha subunit, middle domain superfamily / Translation initiation factor 2, alpha subunit, C-terminal / Eukaryotic translation initiation factor 2 alpha subunit / S1 domain profile. / Ribosomal protein S1-like RNA-binding domain / S1 RNA binding domain ...EIF_2_alpha / Translation initiation factor 2; subunit 1; domain 2 / IF2a, S1-like domain / Translation initiation factor 2, alpha subunit / Translation initiation factor 2, alpha subunit, middle domain superfamily / Translation initiation factor 2, alpha subunit, C-terminal / Eukaryotic translation initiation factor 2 alpha subunit / S1 domain profile. / Ribosomal protein S1-like RNA-binding domain / S1 RNA binding domain / S1 domain / Nucleic acid-binding proteins / DNA polymerase; domain 1 / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Alpha-Beta Plaits / Nucleic acid-binding, OB-fold / Beta Barrel / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Eukaryotic translation initiation factor 2 subunit 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsIto, T. / Marintchev, A. / Wagner, G.
CitationJournal: STRUCTURE / Year: 2004
Title: Solution Structure of Human Initiation Factor eIF2alpha Reveals Homology to the Elongation Factor eEF1B.
Authors: Ito, T. / Marintchev, A. / Wagner, G.
History
DepositionAug 21, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 7, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 27, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Eukaryotic translation initiation factor 2 subunit 1


Theoretical massNumber of molelcules
Total (without water)35,7421
Polymers35,7421
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / 51
RepresentativeModel #1

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Components

#1: Protein Eukaryotic translation initiation factor 2 subunit 1 / Eukaryotic translation initiation factor 2 alpha subunit / eIF-2-alpha / EIF- 2alpha / EIF-2A


Mass: 35741.758 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF2S1 OR EIF2A / Production host: Escherichia coli (E. coli) / References: UniProt: P05198

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionsIonic strength: 1.1 / pH: 7.0 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian VARIAN INOVAVarianVARIAN INOVA7501
Bruker BRUKER DRXBrukerBRUKER DRX6002
Bruker BRUKER DRXBrukerBRUKER DRX5003

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Processing

NMR software
NameVersionDeveloperClassification
NIH-XPLOR12.1JONES,ZOU,COWAN,KJELDGAARDrefinement
NIH-XPLOR12.1JONES,ZOU,COWAN,KJELDGAARDstructure solution
NMR ensembleConformers calculated total number: 51 / Conformers submitted total number: 15

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