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6WL5

Crystal structure of EcmrR C-terminal domain

Summary for 6WL5
Entry DOI10.2210/pdb6wl5/pdb
DescriptorEcmrR transcriptional regulator, CETYL-TRIMETHYL-AMMONIUM, GLYCEROL, ... (6 entities in total)
Functional Keywordstranscriptional factor, transcription
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight77519.41
Authors
Yang, Y.,Liu, C.,Liu, B. (deposition date: 2020-04-18, release date: 2021-04-07, Last modification date: 2024-03-06)
Primary citationYang, Y.,Liu, C.,Zhou, W.,Shi, W.,Chen, M.,Zhang, B.,Schatz, D.G.,Hu, Y.,Liu, B.
Structural visualization of transcription activated by a multidrug-sensing MerR family regulator.
Nat Commun, 12:2702-2702, 2021
Cited by
PubMed Abstract: Bacterial RNA polymerase (RNAP) holoenzyme initiates transcription by recognizing the conserved -35 and -10 promoter elements that are optimally separated by a 17-bp spacer. The MerR family of transcriptional regulators activate suboptimal 19-20 bp spacer promoters in response to myriad cellular signals, ranging from heavy metals to drug-like compounds. The regulation of transcription by MerR family regulators is not fully understood. Here we report one crystal structure of a multidrug-sensing MerR family regulator EcmrR and nine cryo-electron microscopy structures that capture the EcmrR-dependent transcription process from promoter opening to initial transcription to RNA elongation. These structures reveal that EcmrR is a dual ligand-binding factor that reshapes the suboptimal 19-bp spacer DNA to enable optimal promoter recognition, sustains promoter remodeling to stabilize initial transcribing complexes, and finally dissociates from the promoter to reverse DNA remodeling and facilitate the transition to elongation. Our findings yield a comprehensive model for transcription regulation by MerR family factors and provide insights into the transition from transcription initiation to elongation.
PubMed: 33976201
DOI: 10.1038/s41467-021-22990-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

237992

數據於2025-06-25公開中

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