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5GAD

RNC-SRP-SR complex early state

Summary for 5GAD
Entry DOI10.2210/pdb5gad/pdb
EMDB information8000
DescriptorESRP 4.5S RNA, 50S ribosomal protein L9, 50S ribosomal protein L10, ... (40 entities in total)
Functional Keywordsribosome nascent chain, srp, sr, ribosome
Biological sourceEscherichia coli
More
Total number of polymer chains37
Total formula weight1528374.23
Authors
Jomaa, A.,Boehringer, D.,Leibundgut, M.,Ban, N. (deposition date: 2015-11-24, release date: 2016-01-27, Last modification date: 2024-10-16)
Primary citationJomaa, A.,Boehringer, D.,Leibundgut, M.,Ban, N.
Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon.
Nat Commun, 7:10471-10471, 2016
Cited by
PubMed Abstract: Co-translational protein targeting to membranes is a universally conserved process. Central steps include cargo recognition by the signal recognition particle and handover to the Sec translocon. Here we present snapshots of key co-translational-targeting complexes solved by cryo-electron microscopy at near-atomic resolution, establishing the molecular contacts between the Escherichia coli translating ribosome, the signal recognition particle and the translocon. Our results reveal the conformational changes that regulate the latching of the signal sequence, the release of the heterodimeric domains of the signal recognition particle and its receptor, and the handover of the signal sequence to the translocon. We also observe that the signal recognition particle and the translocon insert-specific structural elements into the ribosomal tunnel to remodel it, possibly to sense nascent chains. Our work provides structural evidence for a conformational state of the signal recognition particle and its receptor primed for translocon binding to the ribosome-nascent chain complex.
PubMed: 26804923
DOI: 10.1038/ncomms10471
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.7 Å)
Structure validation

227111

數據於2024-11-06公開中

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