6ZTP

E. coli 70S-RNAP expressome complex in uncoupled state 6

This is a non-PDB format compatible entry.

Summary for 6ZTP

• Entry DOI: 10.2210/pdb6ztp/pdb
• EMDB information: 11423
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (64 entities in total)
• Functional Keywords: transcription, translation, expressome, ribosome, rna polymerase, gene regulation
• Biological source: Escherichia coli; More
• Total number of polymer chains: 62
• Total formula weight: 2631306.43

Authors

Webster, M.W.,Takacs, M.,Weixlbaumer, A. (deposition date: 2020-07-20, release date: 2020-09-16, Last modification date: 2024-04-24)

Primary citation

Webster, M.W.,Takacs, M.,Zhu, C.,Vidmar, V.,Eduljee, A.,Abdelkareem, M.,Weixlbaumer, A.
Structural basis of transcription-translation coupling and collision in bacteria.
Science, 369:1355-1359, 2020

PubMed Abstract: Prokaryotic messenger RNAs (mRNAs) are translated as they are transcribed. The lead ribosome potentially contacts RNA polymerase (RNAP) and forms a supramolecular complex known as the expressome. The basis of expressome assembly and its consequences for transcription and translation are poorly understood. Here, we present a series of structures representing uncoupled, coupled, and collided expressome states determined by cryo-electron microscopy. A bridge between the ribosome and RNAP can be formed by the transcription factor NusG, which stabilizes an otherwise-variable interaction interface. Shortening of the intervening mRNA causes a substantial rearrangement that aligns the ribosome entrance channel to the RNAP exit channel. In this collided complex, NusG linkage is no longer possible. These structures reveal mechanisms of coordination between transcription and translation and provide a framework for future study.

PubMed: 32820062
DOI: 10.1126/science.abb5036

Experimental method

ELECTRON MICROSCOPY (3 Å)