6zto

From Proteopedia

Jump to: navigation, search

E. coli 70S-RNAP expressome complex in uncoupled state 1

Structural highlights

6zto is a 10 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 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

RS17_ECOLI One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. Also plays a role in translational accuracy; neamine-resistant ribosomes show reduced neamine-induced misreading in vitro.[HAMAP-Rule:MF_01345]

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.

Loading citation details..
No citations found

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 6zto

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools