6DV9

Crystal structure of Mycobacterium tuberculosis transcription initiation complex(ECF sigma factor L) containing 5nt RNA with 4nt spacer

Summary for 6DV9

• Entry DOI: 10.2210/pdb6dv9/pdb
• Descriptor: DNA-directed RNA polymerase subunit alpha, ZINC ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
• Functional Keywords: mycobacterium tuberculosis, rna polymerase, ecf sigma factor, transferase, transferase-dna-rna complex, transferase/dna/rna
• Biological source: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv); More
• Total number of polymer chains: 9
• Total formula weight: 400809.97

Authors

Lin, W.,Das, K.,Feng, Y.,Ebright, R.H. (deposition date: 2018-06-23, release date: 2019-02-20, Last modification date: 2024-03-13)

Primary citation

Lin, W.,Mandal, S.,Degen, D.,Cho, M.S.,Feng, Y.,Das, K.,Ebright, R.H.
Structural basis of ECF-sigma-factor-dependent transcription initiation.
Nat Commun, 10:710-710, 2019

PubMed Abstract: Extracytoplasmic (ECF) σ factors, the largest class of alternative σ factors, are related to primary σ factors, but have simpler structures, comprising only two of six conserved functional modules in primary σ factors: region 2 (σR2) and region 4 (σR4). Here, we report crystal structures of transcription initiation complexes containing Mycobacterium tuberculosis RNA polymerase (RNAP), M. tuberculosis ECF σ factor σ, and promoter DNA. The structures show that σR2 and σR4 of the ECF σ factor occupy the same sites on RNAP as in primary σ factors, show that the connector between σR2 and σR4 of the ECF σ factor-although shorter and unrelated in sequence-follows the same path through RNAP as in primary σ factors, and show that the ECF σ factor uses the same strategy to bind and unwind promoter DNA as primary σ factors. The results define protein-protein and protein-DNA interactions involved in ECF-σ-factor-dependent transcription initiation.

PubMed: 30755604
DOI: 10.1038/s41467-019-08443-3

Experimental method

X-RAY DIFFRACTION (3.8 Å)