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PDBsum entry 4u1e
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PDB id:
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Translation
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Title:
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Crystal structure of the eif3b-ctd/eif3i/eif3g-ntd translation initiation complex
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Structure:
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Eukaryotic translation initiation factor 3 subunit i. Chain: i. Synonym: eif3i,eukaryotic translation initiation factor 3 39 kda subunit homolog,eif-3 39 kda subunit homolog. Engineered: yes. Eukaryotic translation initiation factor 3 subunit b. Chain: b. Synonym: eif3b,cell cycle regulation and translation initiation protein,eukaryotic translation initiation factor 3 90 kda subunit,
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 307796. Strain: yjm789. Gene: tif34, scy_4321. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Organism_taxid: 559292. Strain: atcc 204508 / s288c.
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Resolution:
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2.00Å
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R-factor:
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0.187
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R-free:
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0.216
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Authors:
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S.Zhang,J.P.Erzberger,T.Schaefer,N.Ban
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Key ref:
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J.P.Erzberger
et al.
(2014).
Molecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complex.
Cell,
158,
1123-1135.
PubMed id:
DOI:
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Date:
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15-Jul-14
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Release date:
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10-Sep-14
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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Enzyme class:
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Chains B, G:
E.C.?
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DOI no:
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Cell
158:1123-1135
(2014)
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PubMed id:
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Molecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complex.
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J.P.Erzberger,
F.Stengel,
R.Pellarin,
S.Zhang,
T.Schaefer,
C.H.Aylett,
P.Cimermančič,
D.Boehringer,
A.Sali,
R.Aebersold,
N.Ban.
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ABSTRACT
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Eukaryotic translation initiation requires the recruitment of the large,
multiprotein eIF3 complex to the 40S ribosomal subunit. We present X-ray
structures of all major components of the minimal, six-subunit Saccharomyces
cerevisiae eIF3 core. These structures, together with electron microscopy
reconstructions, cross-linking coupled to mass spectrometry, and integrative
structure modeling, allowed us to position and orient all eIF3 components on the
40S⋅eIF1 complex, revealing an extended, modular arrangement of eIF3 subunits.
Yeast eIF3 engages 40S in a clamp-like manner, fully encircling 40S to position
key initiation factors on opposite ends of the mRNA channel, providing a
platform for the recruitment, assembly, and regulation of the translation
initiation machinery. The structures of eIF3 components reported here also have
implications for understanding the architecture of the mammalian 43S
preinitiation complex and the complex of eIF3, 40S, and the hepatitis C internal
ribosomal entry site RNA.
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}
}
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