Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7BL3

pre-50S-ObgE particle state 2

This is a non-PDB format compatible entry.
Summary for 7BL3
Entry DOI10.2210/pdb7bl3/pdb
EMDB information12216
Descriptor23S ribosomal RNA, 50S ribosomal protein L15, 50S ribosomal protein L17, ... (34 entities in total)
Functional Keywordsribosome, pre-50s, ribosome biogenesis, ribosome assembly
Biological sourceEscherichia coli (strain K12)
More
Total number of polymer chains31
Total formula weight1397981.06
Authors
Hilal, T.,Nikolay, R.,Spahn, C.M.T. (deposition date: 2021-01-18, release date: 2021-05-12, Last modification date: 2024-10-23)
Primary citationNikolay, R.,Hilal, T.,Schmidt, S.,Qin, B.,Schwefel, D.,Vieira-Vieira, C.H.,Mielke, T.,Burger, J.,Loerke, J.,Amikura, K.,Flugel, T.,Ueda, T.,Selbach, M.,Deuerling, E.,Spahn, C.M.T.
Snapshots of native pre-50S ribosomes reveal a biogenesis factor network and evolutionary specialization.
Mol.Cell, 81:1200-1215.e9, 2021
Cited by
PubMed Abstract: Ribosome biogenesis is a fundamental multi-step cellular process that culminates in the formation of ribosomal subunits, whose production and modification are regulated by numerous biogenesis factors. In this study, we analyze physiologic prokaryotic ribosome biogenesis by isolating bona fide pre-50S subunits from an Escherichia coli strain with the biogenesis factor ObgE, affinity tagged at its native gene locus. Our integrative structural approach reveals a network of interacting biogenesis factors consisting of YjgA, RluD, RsfS, and ObgE on the immature pre-50S subunit. In addition, our study provides mechanistic insight into how the GTPase ObgE, in concert with other biogenesis factors, facilitates the maturation of the 50S functional core and reveals both conserved and divergent evolutionary features of ribosome biogenesis between prokaryotes and eukaryotes.
PubMed: 33639093
DOI: 10.1016/j.molcel.2021.02.006
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

227111

数据于2024-11-06公开中

PDB statisticsPDBj update infoContact PDBjnumon