7oif

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CspA-27 cotranslational folding intermediate 2

Structural highlights

7oif is a 10 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3Å
Ligands:0TD, 1MG, 2MA, 2MG, 3TD, 4OC, 5MC, 5MU, 6MZ, FME, G7M, MA6, MG, OMC, OMG, OMU, PSU, UR3, ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RS7_ECOLI One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, where it has been shown to contact mRNA. Has been shown to contact tRNA in both the P and E sites; it probably blocks exit of the E site tRNA.[1] Protein S7 is also a translational repressor protein; it regulates the expression of the str operon members to different degrees by binding to its mRNA.[2]

Publication Abstract from PubMed

Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of nascent chains is not only shaped by their amino acid sequence but also by the interactions with the ribosome. Here, we combine biophysical methods with cryo-EM structure determination to show that folding of a beta-barrel protein begins with formation of a dynamic alpha-helix inside the ribosome. As the growing peptide reaches the end of the tunnel, the N-terminal part of the nascent chain refolds to a beta-hairpin structure that remains dynamic until its release from the ribosome. Contacts with the ribosome and structure of the peptidyl transferase center depend on nascent chain conformation. These results indicate that proteins may start out as alpha-helices inside the tunnel and switch into their native folds only as they emerge from the ribosome. Moreover, the correlation of nascent chain conformations with reorientation of key residues of the ribosomal peptidyl-transferase center suggest that protein folding could modulate ribosome activity.

A switch from alpha-helical to beta-strand conformation during co-translational protein folding.,Agirrezabala X, Samatova E, Macher M, Liutkute M, Maiti M, Gil-Carton D, Novacek J, Valle M, Rodnina MV EMBO J. 2022 Feb 15;41(4):e109175. doi: 10.15252/embj.2021109175. Epub 2022 Jan , 7. PMID:34994471[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
4 reviews cite this structure
Protein folding problem: enigma, paradox, solution.
Finkelstein et al. (2022)
3 more
11 other articles
No citations found

See Also

References

  1. ↑ Nowotny V, Nierhaus KH. Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry. 1988 Sep 6;27(18):7051-5. PMID:2461734
  2. ↑ Nowotny V, Nierhaus KH. Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry. 1988 Sep 6;27(18):7051-5. PMID:2461734
  3. ↑ Agirrezabala X, Samatova E, Macher M, Liutkute M, Maiti M, Gil-Carton D, Novacek J, Valle M, Rodnina MV. A switch from α-helical to β-strand conformation during co-translational protein folding. EMBO J. 2022 Feb 15;41(4):e109175. PMID:34994471 doi:10.15252/embj.2021109175

Contents


PDB ID 7oif

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