6ztm

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E. coli 70S-RNAP expressome complex in collided state without NusG

Structural highlights

6ztm is a 10 chain structure with sequence from Escherichia coli and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.3Å
Ligands:1MG, 2MA, 2MG, 3AU, 3TD, 4D4, 4OC, 4SU, 5MC, 5MU, 6MZ, 7MG, D2T, G7M, H2U, MA6, MEQ, MG, MIA, OMC, OMG, OMU, PHE, PSU, UR3, ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL33_ECOLI

Publication Abstract from PubMed

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.

Structural basis of transcription-translation coupling and collision in bacteria.,Webster MW, Takacs M, Zhu C, Vidmar V, Eduljee A, Abdelkareem M, Weixlbaumer A Science. 2020 Sep 11;369(6509):1355-1359. doi: 10.1126/science.abb5036. Epub 2020, Aug 20. PMID:32820062[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. Webster MW, Takacs M, Zhu C, Vidmar V, Eduljee A, Abdelkareem M, Weixlbaumer A. Structural basis of transcription-translation coupling and collision in bacteria. Science. 2020 Sep 11;369(6509):1355-1359. PMID:32820062 doi:10.1126/science.abb5036

Contents


PDB ID 6ztm

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OCA

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