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6XH7

CueR-TAC without RNA

Summary for 6XH7
Entry DOI10.2210/pdb6xh7/pdb
Related6XH8
EMDB information22184 22185 22289
DescriptorDNA-directed RNA polymerase subunit alpha, COPPER (II) ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
Functional Keywordstranscription activation, rna polymerase, merr-family, transcription, transcription-dna complex, transcription/dna
Biological sourceEscherichia coli
More
Total number of polymer chains10
Total formula weight528025.69
Authors
Liu, B.,Shi, W.,Yang, Y. (deposition date: 2020-06-18, release date: 2021-04-14, Last modification date: 2024-03-06)
Primary citationShi, W.,Zhang, B.,Jiang, Y.,Liu, C.,Zhou, W.,Chen, M.,Yang, Y.,Hu, Y.,Liu, B.
Structural basis of copper-efflux-regulator-dependent transcription activation.
Iscience, 24:102449-102449, 2021
Cited by
PubMed Abstract: The copper efflux regulator (CueR), a representative member of mercury resistance regulator (MerR) family metalloregulators, controls expression of copper homeostasis-regulating genes in bacteria. The mechanism of transcription activation by CueR and other MerR family regulators is bending the spacer domain of promoter DNA. Here, we report the cryo-EM structures of the intact CueR-dependent transcription activation complexes. The structures show that CueR dimer bends the 19-bp promoter spacer to realign the -35 and -10 elements for recognition by σ-RNA polymerase holoenzyme and reveal a previously unreported interaction between the DNA-binding domain (DBD) from one CueR subunit and the σ nonconserved region (σNCR). Functional studies have shown that the CueR-σNCR interaction plays an auxiliary role in CueR-dependent transcription, assisting the activation mechanism of bending promoter DNA by CueR dimer. Because DBDs are highly conserved in sequence and structure, this transcription-activating mechanism could be generally used by MerR family regulators.
PubMed: 34113812
DOI: 10.1016/j.isci.2021.102449
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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