5TBZ

E. Coli RNA Polymerase complexed with NusG

Summary for 5TBZ

• Entry DOI: 10.2210/pdb5tbz/pdb
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (4 entities in total)
• Functional Keywords: transcription elongation, rna polymerase, nusg, transcription-rna complex, transcription/rna
• Biological source: Escherichia coli O157:H7; More
• Total number of polymer chains: 10
• Total formula weight: 761094.65

Authors

Liu, B.,Steitz, T.A. (deposition date: 2016-09-13, release date: 2016-12-07, Last modification date: 2024-10-30)

Primary citation

Liu, B.,Steitz, T.A.
Structural insights into NusG regulating transcription elongation.
Nucleic Acids Res., 45:968-974, 2017

PubMed Abstract: NusG is an essential transcription factor that plays multiple key regulatory roles in transcription elongation, termination and coupling translation and transcription. The core role of NusG is to enhance transcription elongation and RNA polymerase processivity. Here, we present the structure of Escherichia coli RNA polymerase complexed with NusG. The structure shows that the NusG N-terminal domain (NGN) binds at the central cleft of RNA polymerase surrounded by the β' clamp helices, the β protrusion, and the β lobe domains to close the promoter DNA binding channel and constrain the β' clamp domain, but with an orientation that is different from the one observed in the archaeal β' clamp-Spt4/5 complex. The structure also allows us to construct a reliable model of the complete NusG-associated transcription elongation complex, suggesting that the NGN domain binds at the upstream fork junction of the transcription elongation complex, similar to σ2 in the transcription initiation complex, to stabilize the junction, and therefore enhances transcription processivity.

PubMed: 27899640
DOI: 10.1093/nar/gkw1159

Experimental method

X-RAY DIFFRACTION (7 Å)