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6JCX

Mycobacterium tuberculosis transcription initiation complex with ECF sigma factor sigma H and 6nt RNA

Summary for 6JCX
Entry DOI10.2210/pdb6jcx/pdb
DescriptorDNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (11 entities in total)
Functional Keywordsmycobacterium tuberculosis, rna polymerase, sigma h, transcription initiation, transcription
Biological sourceMycobacterium tuberculosis H37Rv
More
Total number of polymer chains9
Total formula weight408826.73
Authors
Li, L.,Zhang, Y. (deposition date: 2019-01-30, release date: 2019-05-29, Last modification date: 2023-11-22)
Primary citationFang, C.,Li, L.,Shen, L.,Shi, J.,Wang, S.,Feng, Y.,Zhang, Y.
Structures and mechanism of transcription initiation by bacterial ECF factors.
Nucleic Acids Res., 47:7094-7104, 2019
Cited by
PubMed Abstract: Bacterial RNA polymerase (RNAP) forms distinct holoenzymes with extra-cytoplasmic function (ECF) σ factors to initiate specific gene expression programs. In this study, we report a cryo-EM structure at 4.0 Å of Escherichia coli transcription initiation complex comprising σE-the most-studied bacterial ECF σ factor (Ec σE-RPo), and a crystal structure at 3.1 Å of Mycobacterium tuberculosis transcription initiation complex with a chimeric σH/E (Mtb σH/E-RPo). The structure of Ec σE-RPo reveals key interactions essential for assembly of E. coli σE-RNAP holoenzyme and for promoter recognition and unwinding by E. coli σE. Moreover, both structures show that the non-conserved linkers (σ2/σ4 linker) of the two ECF σ factors are inserted into the active-center cleft and exit through the RNA-exit channel. We performed secondary-structure prediction of 27,670 ECF σ factors and find that their non-conserved linkers probably reach into and exit from RNAP active-center cleft in a similar manner. Further biochemical results suggest that such σ2/σ4 linker plays an important role in RPo formation, abortive production and promoter escape during ECF σ factors-mediated transcription initiation.
PubMed: 31131408
DOI: 10.1093/nar/gkz470
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.903 Å)
Structure validation

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数据于2024-11-06公开中

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