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Structure paper

TitleDecoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.
Journal, issue, pagesCell, Vol. 167, Issue 5, Page 1229-1240.e15, Year 2016
Publish dateNov 17, 2016
AuthorsSichen Shao / Jason Murray / Alan Brown / Jack Taunton / V Ramakrishnan / Ramanujan S Hegde /
PubMed AbstractIn eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the ...In eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the mammalian ribosome engaged with decoding factor⋅GTPase complexes representing intermediates of translation elongation (aminoacyl-tRNA⋅eEF1A), termination (eRF1⋅eRF3), and ribosome rescue (Pelota⋅Hbs1l). Comparative analyses reveal that each decoding factor exploits the plasticity of the ribosomal decoding center to differentially remodel ribosomal proteins and rRNA. This leads to varying degrees of large-scale ribosome movements and implies distinct mechanisms for communicating information from the decoding center to each GTPase. Additional structural snapshots of the translation termination pathway reveal the conformational changes that choreograph the accommodation of decoding factors into the peptidyl transferase center. Our results provide a structural framework for how different states of the mammalian ribosome are selectively recognized by the appropriate decoding factor⋅GTPase complex to ensure translational fidelity.
External linksCell / PubMed:27863242 / PubMed Central
MethodsEM (single particle)
Resolution3.06 - 3.99 Å
Structure data

EMDB-4129:
Structure of the mammalian ribosome with P- and E-site tRNAs and an unoccupied A site
Method: EM (single particle) / Resolution: 3.06 Å

EMDB-4130, PDB-5lzs:
Structure of the mammalian ribosomal elongation complex with aminoacyl-tRNA, eEF1A, and didemnin B
Method: EM (single particle) / Resolution: 3.31 Å

EMDB-4131, PDB-5lzt:
Structure of the mammalian ribosomal termination complex with eRF1 and eRF3.
Method: EM (single particle) / Resolution: 3.65 Å

EMDB-4132, PDB-5lzu:
Structure of the mammalian ribosomal termination complex with accommodated eRF1
Method: EM (single particle) / Resolution: 3.75 Å

EMDB-4133, PDB-5lzv:
Structure of the mammalian ribosomal termination complex with accommodated eRF1(AAQ) and ABCE1.
Method: EM (single particle) / Resolution: 3.35 Å

EMDB-4134, PDB-5lzw:
Structure of the mammalian rescue complex with Pelota and Hbs1l assembled on a truncated mRNA.
Method: EM (single particle) / Resolution: 3.53 Å

EMDB-4135, PDB-5lzx:
Structure of the mammalian rescue complex with Pelota and Hbs1l assembled on a UGA stop codon.
Method: EM (single particle) / Resolution: 3.67 Å

EMDB-4136, PDB-5lzy:
Structure of the mammalian rescue complex with Pelota and Hbs1l assembled on a polyadenylated mRNA.
Method: EM (single particle) / Resolution: 3.99 Å

EMDB-4137, PDB-5lzz:
Structure of the mammalian rescue complex with Pelota and Hbs1l (combined)
Method: EM (single particle) / Resolution: 3.47 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

ChemComp-7C4:
(2~{S})-~{N}-[(2~{R})-1-[[(3~{S},6~{S},8~{S},12~{S},13~{R},16~{S},17~{R},20~{S},23~{S})-13-[(2~{S})-butan-2-yl]-20-[(4-methoxyphenyl)methyl]-6,17,21-trimethyl-3-(2-methylpropyl)-12-oxidanyl-2,5,7,10,15,19,22-heptakis(oxidanylidene)-8-propan-2-yl-9,18-dioxa-1,4,14,21-tetrazabicyclo[21.3.0]hexacosan-16-yl]amino]-4-methyl-1-oxidanylidene-pentan-2-yl]-~{N}-methyl-1-[(2~{S})-2-oxidanylpropanoyl]pyrrolidine-2-carboxamide

ChemComp-GCP:
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-PCP, energy-carrying molecule analogue*YM

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

Source
  • oryctolagus cuniculus (rabbit)
  • Rabbit (rabbit)
  • homo sapiens (human)
KeywordsRIBOSOME / Translation / Elongation

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