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Structure paper

TitleFolding pathway of an Ig domain is conserved on and off the ribosome.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 115, Issue 48, Page E11284-E11293, Year 2018
Publish dateNov 27, 2018
AuthorsPengfei Tian / Annette Steward / Renuka Kudva / Ting Su / Patrick J Shilling / Adrian A Nickson / Jeffrey J Hollins / Roland Beckmann / Gunnar von Heijne / Jane Clarke / Robert B Best /
PubMed AbstractProteins that fold cotranslationally may do so in a restricted configurational space, due to the volume occupied by the ribosome. How does this environment, coupled with the close proximity of the ...Proteins that fold cotranslationally may do so in a restricted configurational space, due to the volume occupied by the ribosome. How does this environment, coupled with the close proximity of the ribosome, affect the folding pathway of a protein? Previous studies have shown that the cotranslational folding process for many proteins, including small, single domains, is directly affected by the ribosome. Here, we investigate the cotranslational folding of an all-β Ig domain, titin I27. Using an arrest peptide-based assay and structural studies by cryo-EM, we show that I27 folds in the mouth of the ribosome exit tunnel. Simulations that use a kinetic model for the force dependence of escape from arrest accurately predict the fraction of folded protein as a function of length. We used these simulations to probe the folding pathway on and off the ribosome. Our simulations-which also reproduce experiments on mutant forms of I27-show that I27 folds, while still sequestered in the mouth of the ribosome exit tunnel, by essentially the same pathway as free I27, with only subtle shifts of critical contacts from the C to the N terminus.
External linksProc Natl Acad Sci U S A / PubMed:30413621 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

0322

6i0y

EMDB-0322, PDB-6i0y:
TnaC-stalled ribosome complex with the titin I27 domain folding close to the ribosomal exit tunnel
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-TRP:
TRYPTOPHAN

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • homo sapiens (human)
KeywordsRIBOSOME / Protein folding / ribosomal exit tunnel / nascent chain / titin I27 domain

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