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Structure paper

TitleStructural basis of early translocation events on the ribosome.
Journal, issue, pagesNature, Vol. 595, Issue 7869, Page 741-745, Year 2021
Publish dateJul 7, 2021
AuthorsEmily J Rundlet / Mikael Holm / Magdalena Schacherl / S Kundhavai Natchiar / Roger B Altman / Christian M T Spahn / Alexander G Myasnikov / Scott C Blanchard /
PubMed AbstractPeptide-chain elongation during protein synthesis entails sequential aminoacyl-tRNA selection and translocation reactions that proceed rapidly (2-20 per second) and with a low error rate (around ...Peptide-chain elongation during protein synthesis entails sequential aminoacyl-tRNA selection and translocation reactions that proceed rapidly (2-20 per second) and with a low error rate (around 10 to 10 at each step) over thousands of cycles. The cadence and fidelity of ribosome transit through mRNA templates in discrete codon increments is a paradigm for movement in biological systems that must hold for diverse mRNA and tRNA substrates across domains of life. Here we use single-molecule fluorescence methods to guide the capture of structures of early translocation events on the bacterial ribosome. Our findings reveal that the bacterial GTPase elongation factor G specifically engages spontaneously achieved ribosome conformations while in an active, GTP-bound conformation to unlock and initiate peptidyl-tRNA translocation. These findings suggest that processes intrinsic to the pre-translocation ribosome complex can regulate the rate of protein synthesis, and that energy expenditure is used later in the translocation mechanism than previously proposed.
External linksNature / PubMed:34234344 / PubMed Central
MethodsEM (single particle)
Resolution2.33 - 2.72 Å
Structure data

24120

7n1p

EMDB-24120, PDB-7n1p:
Elongating 70S ribosome complex in a classical pre-translocation (PRE-C) conformation
Method: EM (single particle) / Resolution: 2.33 Å

24132

7n2c

EMDB-24132, PDB-7n2c:
Elongating 70S ribosome complex in a fusidic acid-stalled intermediate state of translocation bound to EF-G(GDP) (INT2)
Method: EM (single particle) / Resolution: 2.72 Å

24133

7n2u

EMDB-24133, PDB-7n2u:
Elongating 70S ribosome complex in a hybrid-H1 pre-translocation (PRE-H1) conformation
Method: EM (single particle) / Resolution: 2.53 Å

24134

7n2v

EMDB-24134, PDB-7n2v:
Elongating 70S ribosome complex in a spectinomycin-stalled intermediate state of translocation bound to EF-G in an active, GTP conformation (INT1)
Method: EM (single particle) / Resolution: 2.54 Å

24135

7n30

EMDB-24135, PDB-7n30:
Elongating 70S ribosome complex in a hybrid-H2* pre-translocation (PRE-H2*) conformation
Method: EM (single particle) / Resolution: 2.66 Å

24136

7n31

EMDB-24136, PDB-7n31:
Elongating 70S ribosome complex in a post-translocation (POST) conformation
Method: EM (single particle) / Resolution: 2.69 Å

Chemicals

ChemComp-PUT:
1,4-DIAMINOBUTANE

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-SPD:
SPERMIDINE

ChemComp-HOH:
WATER

ChemComp-FUA:
FUSIDIC ACID / antibiotic, Antimicrobial*YM

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

ChemComp-SCM:
SPECTINOMYCIN / antibiotic*YM

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

Source
  • escherichia coli k-12 (bacteria)
  • escherichia coli bl21 (bacteria)
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli (E. coli)
KeywordsRIBOSOME / Elongation complex / tRNA / mRNA / Pre-translocation / translocation / EF-G & GTP / 70S ribosome / post-translocation

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