7YPA
Cryo-EM structure of Escherichia coli hairpin-nucleation complex of transcription termination (TTC-hairpin)
Summary for 7YPA
Entry DOI | 10.2210/pdb7ypa/pdb |
EMDB information | 33997 |
Descriptor | DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total) |
Functional Keywords | termination, intrinsic termination, hairpin nucleation, factor-independent termination, pre-termination, transcription-dna-rna complex, transcription/dna/rna |
Biological source | Escherichia coli K-12 More |
Total number of polymer chains | 9 |
Total formula weight | 419546.01 |
Authors | |
Primary citation | You, L.,Omollo, E.O.,Yu, C.,Mooney, R.A.,Shi, J.,Shen, L.,Wu, X.,Wen, A.,He, D.,Zeng, Y.,Feng, Y.,Landick, R.,Zhang, Y. Structural basis for intrinsic transcription termination. Nature, 613:783-789, 2023 Cited by PubMed Abstract: Efficient and accurate termination is required for gene transcription in all living organisms. Cellular RNA polymerases in both bacteria and eukaryotes can terminate their transcription through a factor-independent termination pathway-called intrinsic termination transcription in bacteria-in which RNA polymerase recognizes terminator sequences, stops nucleotide addition and releases nascent RNA spontaneously. Here we report a set of single-particle cryo-electron microscopy structures of Escherichia coli transcription intrinsic termination complexes representing key intermediate states of the event. The structures show how RNA polymerase pauses at terminator sequences, how the terminator RNA hairpin folds inside RNA polymerase, and how RNA polymerase rewinds the transcription bubble to release RNA and then DNA. These macromolecular snapshots define a structural mechanism for bacterial intrinsic termination and a pathway for RNA release and DNA collapse that is relevant for factor-independent termination by all RNA polymerases. PubMed: 36631609DOI: 10.1038/s41586-022-05604-1 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.05 Å) |
Structure validation
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