6JCX
Mycobacterium tuberculosis transcription initiation complex with ECF sigma factor sigma H and 6nt RNA
Summary for 6JCX
Entry DOI | 10.2210/pdb6jcx/pdb |
Descriptor | DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (11 entities in total) |
Functional Keywords | mycobacterium tuberculosis, rna polymerase, sigma h, transcription initiation, transcription |
Biological source | Mycobacterium tuberculosis H37Rv More |
Total number of polymer chains | 9 |
Total formula weight | 408826.73 |
Authors | |
Primary citation | Fang, 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: 31131408DOI: 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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