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PDBsum entry 6tqn

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Top Page protein dna_rna metals Protein-protein interface(s) links
Transcription PDB id
6tqn
Contents
Protein chains
255 a.a.
495 a.a.
134 a.a.
98 a.a.
178 a.a.
322 a.a.
222 a.a.
90 a.a.
1342 a.a.
1337 a.a.
DNA/RNA
Metals
_MG ×3
_ZN ×2

References listed in PDB file
Key reference
Title Structure-Based mechanisms of a molecular RNA polymerase/chaperone machine required for ribosome biosynthesis.
Authors Y.H.Huang, T.Hilal, B.Loll, J.Bürger, T.Mielke, C.Böttcher, N.Said, M.C.Wahl.
Ref. Mol Cell, 2020, 79, 1024. [DOI no: 10.1016/j.molcel.2020.08.010]
PubMed id 32871103
Abstract
Bacterial ribosomal RNAs are synthesized by a dedicated, conserved transcription-elongation complex that transcribes at high rates, shields RNA polymerase from premature termination, and supports co-transcriptional RNA folding, modification, processing, and ribosomal subunit assembly by presently unknown mechanisms. We have determined cryo-electron microscopy structures of complete Escherichia coli ribosomal RNA transcription elongation complexes, comprising RNA polymerase; DNA; RNA bearing an N-utilization-site-like anti-termination element; Nus factors A, B, E, and G; inositol mono-phosphatase SuhB; and ribosomal protein S4. Our structures and structure-informed functional analyses show that fast transcription and anti-termination involve suppression of NusA-stabilized pausing, enhancement of NusG-mediated anti-backtracking, sequestration of the NusG C-terminal domain from termination factor ρ, and the ρ blockade. Strikingly, the factors form a composite RNA chaperone around the RNA polymerase RNA-exit tunnel, which supports co-transcriptional RNA folding and annealing of distal RNA regions. Our work reveals a polymerase/chaperone machine required for biosynthesis of functional ribosomes.
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