6QDW

Cryo-EM structure of the 50S ribosomal subunit at 2.83 Angstroms with modeled GBC SecM peptide

Summary for 6QDW

• Entry DOI: 10.2210/pdb6qdw/pdb
• EMDB information: 4531
• Descriptor: 50S ribosomal protein L28, 23S rRNA, 50S ribosomal protein L2, ... (32 entities in total)
• Functional Keywords: translation, 50s ribosome, nascent peptide chain, ribosome
• Biological source: Bos taurus (Bovine); More
• Total number of polymer chains: 32
• Total formula weight: 1374472.24

Authors

Schulte, L.,Reitz, J.,Hodirnau, V.V.,Kudlinzki, D.,Mao, J.,Glaubitz, C.,Frangakis, A.,Schwalbe, H. (deposition date: 2019-01-03, release date: 2020-01-15, Last modification date: 2024-11-20)

Primary citation

Schulte, L.,Mao, J.,Reitz, J.,Sreeramulu, S.,Kudlinzki, D.,Hodirnau, V.V.,Meier-Credo, J.,Saxena, K.,Buhr, F.,Langer, J.D.,Blackledge, M.,Frangakis, A.S.,Glaubitz, C.,Schwalbe, H.
Cysteine oxidation and disulfide formation in the ribosomal exit tunnel.
Nat Commun, 11:5569-5569, 2020

PubMed Abstract: Understanding the conformational sampling of translation-arrested ribosome nascent chain complexes is key to understand co-translational folding. Up to now, coupling of cysteine oxidation, disulfide bond formation and structure formation in nascent chains has remained elusive. Here, we investigate the eye-lens protein γB-crystallin in the ribosomal exit tunnel. Using mass spectrometry, theoretical simulations, dynamic nuclear polarization-enhanced solid-state nuclear magnetic resonance and cryo-electron microscopy, we show that thiol groups of cysteine residues undergo S-glutathionylation and S-nitrosylation and form non-native disulfide bonds. Thus, covalent modification chemistry occurs already prior to nascent chain release as the ribosome exit tunnel provides sufficient space even for disulfide bond formation which can guide protein folding.

PubMed: 33149120
DOI: 10.1038/s41467-020-19372-x

Experimental method

ELECTRON MICROSCOPY (2.83 Å)