Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Visualization of translation and protein biogenesis at the ER membrane.
Journal, issue, pages	Nature, Vol. 614, Issue 7946, Page 160-167, Year 2023
Publish date	Jan 25, 2023
Authors	Max Gemmer / Marten L Chaillet / Joyce van Loenhout / Rodrigo Cuevas Arenas / Dimitrios Vismpas / Mariska Gröllers-Mulderij / Fujiet A Koh / Pascal Albanese / Richard A Scheltema / Stuart C Howes / Abhay Kotecha / Juliette Fedry / Friedrich Förster /
PubMed Abstract	The dynamic ribosome-translocon complex, which resides at the endoplasmic reticulum (ER) membrane, produces a major fraction of the human proteome. It governs the synthesis, translocation, membrane ...The dynamic ribosome-translocon complex, which resides at the endoplasmic reticulum (ER) membrane, produces a major fraction of the human proteome. It governs the synthesis, translocation, membrane insertion, N-glycosylation, folding and disulfide-bond formation of nascent proteins. Although individual components of this machinery have been studied at high resolution in isolation, insights into their interplay in the native membrane remain limited. Here we use cryo-electron tomography, extensive classification and molecular modelling to capture snapshots of mRNA translation and protein maturation at the ER membrane at molecular resolution. We identify a highly abundant classical pre-translocation intermediate with eukaryotic elongation factor 1a (eEF1a) in an extended conformation, suggesting that eEF1a may remain associated with the ribosome after GTP hydrolysis during proofreading. At the ER membrane, distinct polysomes bind to different ER translocons specialized in the synthesis of proteins with signal peptides or multipass transmembrane proteins with the translocon-associated protein complex (TRAP) present in both. The near-complete atomic model of the most abundant ER translocon variant comprising the protein-conducting channel SEC61, TRAP and the oligosaccharyltransferase complex A (OSTA) reveals specific interactions of TRAP with other translocon components. We observe stoichiometric and sub-stoichiometric cofactors associated with OSTA, which are likely to include protein isomerases. In sum, we visualize ER-bound polysomes with their coordinated downstream machinery.
External links	Nature / PubMed:36697828 / PubMed Central
Methods	EM (subtomogram averaging) / EM (single particle)
Resolution	2.9 - 9.3 Å
Structure data	15870 8b6l EMDB-15870, PDB-8b6l: Subtomogram average of the human Sec61-TRAP-OSTA-translocon Method: EM (subtomogram averaging) / Resolution: 7.6 Å EMDB-15871: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Decoding-Sampling State Method: EM (subtomogram averaging) / Resolution: 4.8 Å EMDB-15872: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Classical Pre+ State Method: EM (subtomogram averaging) / Resolution: 4.6 Å EMDB-15873: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Classical Pre State Method: EM (subtomogram averaging) / Resolution: 8.0 Å EMDB-15874: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Rotated-1 Pre+ State Method: EM (subtomogram averaging) / Resolution: 6.7 Å EMDB-15875: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Rotated-1 Pre State Method: EM (subtomogram averaging) / Resolution: 6.1 Å EMDB-15876: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Rotated-2 Pre State Method: EM (subtomogram averaging) / Resolution: 4.8 Å EMDB-15877: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Translocation State Method: EM (subtomogram averaging) / Resolution: 6.8 Å EMDB-15878: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Post State Method: EM (subtomogram averaging) / Resolution: 5.9 Å EMDB-15879: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Non-Rotated Hibernating State Method: EM (subtomogram averaging) / Resolution: 6.5 Å EMDB-15880: Subtomogram Average of Soluble and ER Membrane-Associated Ribosomes in the Rotated Hibernating State Method: EM (subtomogram averaging) / Resolution: 6.7 Å EMDB-15884: Subtomogram Average of the Ribosome-Sec61-TRAP-OSTA-Translocon Complex Method: EM (subtomogram averaging) / Resolution: 4.5 Å EMDB-15885: Subtomogram Average of the Ribosome-Sec61-TRAP-Translocon Complex Method: EM (subtomogram averaging) / Resolution: 6.5 Å EMDB-15886: Subtomogram Average of the Ribosome-Sec61-TRAP-Multipass-Translocon Complex Method: EM (subtomogram averaging) / Resolution: 7.5 Å EMDB-15887: Subtomogram Average of the Ribosome-Sec61-Multipass-Translocon Complex Method: EM (subtomogram averaging) / Resolution: 6.7 Å EMDB-15888: Subtomogram Average of the Ribosome-EBP1 Complex Method: EM (subtomogram averaging) / Resolution: 5.0 Å EMDB-15889: Subtomogram Average of the Idle Ribosome-Sec61-TRAP-OSTA-Translocon Complex Method: EM (subtomogram averaging) / Resolution: 6.4 Å EMDB-15890: Subtomogram Average of the Sec61-TRAP-OSTA Translocon Method: EM (subtomogram averaging) / Resolution: 9.3 Å EMDB-15891: Subtomogram Average of the Sec61-TRAP-OSTA-L1 Translocon Method: EM (subtomogram averaging) / Resolution: 8.2 Å EMDB-15892: Subtomogram Average of the Sec61-TRAP-OSTA-L2 Translocon Method: EM (subtomogram averaging) / Resolution: 8.3 Å 15893 8b6z EMDB-15893, PDB-8b6z: CryoEM Structure of Extended eEF1A bound to the Ribosome in the Classical Pre State Method: EM (single particle) / Resolution: 2.9 Å
Source	homo sapiens (human) human (human)
Keywords	MEMBRANE PROTEIN / membrane protein complex / protein translocation / N-glycosylation / signal peptide insertion / RIBOSOME / translation / protein biogenesis / elongation factor