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PDBsum entry 3j8c
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Contents |
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488 a.a.
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546 a.a.
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384 a.a.
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232 a.a.
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254 a.a.
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204 a.a.
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258 a.a.
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176 a.a.
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PDB id:
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Translation
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Title:
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Model of the human eif3 pci-mpn octamer docked into the 43s em map
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Structure:
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Eukaryotic translation initiation factor 3 subunit a. Chain: a. Fragment: see remark 999. Synonym: eif3a, eukaryotic translation initiation factor 3 subunit 10, eif-3-theta, eif3 p167, eif3 p180, eif3 p185. Eukaryotic translation initiation factor 3 subunit c. Chain: c. Fragment: see remark 999. Synonym: eif3c, eukaryotic translation initiation factor 3 subunit 8,
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
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Authors:
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J.P.Erzberger,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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08-Oct-14
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Release date:
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22-Oct-14
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Supersedes:
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PROCHECK
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Headers
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References
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Q14152
(EIF3A_HUMAN) -
Eukaryotic translation initiation factor 3 subunit A from Homo sapiens
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Seq: Struc:
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1382 a.a.
488 a.a.*
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Q99613
(EIF3C_HUMAN) -
Eukaryotic translation initiation factor 3 subunit C from Homo sapiens
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Seq: Struc:
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913 a.a.
546 a.a.*
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P60228
(EIF3E_HUMAN) -
Eukaryotic translation initiation factor 3 subunit E from Homo sapiens
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Seq: Struc:
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445 a.a.
384 a.a.*
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O00303
(EIF3F_HUMAN) -
Eukaryotic translation initiation factor 3 subunit F from Homo sapiens
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Seq: Struc:
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357 a.a.
232 a.a.*
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O15372
(EIF3H_HUMAN) -
Eukaryotic translation initiation factor 3 subunit H from Homo sapiens
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Seq: Struc:
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352 a.a.
254 a.a.*
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Q9UBQ5
(EIF3K_HUMAN) -
Eukaryotic translation initiation factor 3 subunit K from Homo sapiens
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Seq: Struc:
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218 a.a.
204 a.a.*
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Enzyme class:
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Chain F:
E.C.3.4.19.12
- ubiquitinyl hydrolase 1.
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Reaction:
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Thiol-dependent hydrolysis of ester, thiolester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
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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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