6M6B

Cryo-EM structure of Thermus thermophilus Mfd in complex with RNA polymerase and ATP-gamma-S

Summary for 6M6B

• Entry DOI: 10.2210/pdb6m6b/pdb
• EMDB information: 30118
• Descriptor: DNA-directed RNA polymerase subunit alpha, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
• Functional Keywords: transcription, rna polymerase, dna repair, mfd
• Biological source: Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039); More
• Total number of polymer chains: 8
• Total formula weight: 527288.78

Authors

Shi, J.,Wen, A.,Feng, Y. (deposition date: 2020-03-14, release date: 2020-10-14, Last modification date: 2025-06-18)

Primary citation

Shi, J.,Wen, A.,Zhao, M.,Jin, S.,You, L.,Shi, Y.,Dong, S.,Hua, X.,Zhang, Y.,Feng, Y.
Structural basis of Mfd-dependent transcription termination.
Nucleic Acids Res., 48:11762-11772, 2020

PubMed Abstract: Mfd-dependent transcription termination plays an important role in transcription-coupled DNA repair, transcription-replication conflict resolution, and antimicrobial resistance development. Despite extensive studies, the molecular mechanism of Mfd-dependent transcription termination in bacteria remains unclear, with several long-standing puzzles. How Mfd is activated by stalled RNA polymerase (RNAP) and how activated Mfd translocates along the DNA are unknown. Here, we report the single-particle cryo-electron microscopy structures of T. thermophilus Mfd-RNAP complex with and without ATPγS. The structures reveal that Mfd undergoes profound conformational changes upon activation, contacts the RNAP β1 domain and its clamp, and pries open the RNAP clamp. These structures provide a foundation for future studies aimed at dissecting the precise mechanism of Mfd-dependent transcription termination and pave the way for rational drug design targeting Mfd for the purpose of tackling the antimicrobial resistance crisis.

PubMed: 33068413
DOI: 10.1093/nar/gkaa904

Experimental method

ELECTRON MICROSCOPY (4.1 Å)