6DVD
Crystal structure of Mycobacterium tuberculosis transcription initiation complex(ECF sigma factor L) with 6 nt spacer and bromine labelled in position "-11
Summary for 6DVD
| Entry DOI | 10.2210/pdb6dvd/pdb |
| Descriptor | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (8 entities in total) |
| Functional Keywords | mycobacterium tuberculosis, rna polymerase, ecf sigma factor, transferase, transferase-dna complex, transferase/dna |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) More |
| Total number of polymer chains | 8 |
| Total formula weight | 397609.65 |
| 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 Cited by 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: 30755604DOI: 10.1038/s41467-019-08443-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.899 Å) |
Structure validation
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