Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6JHE

Crystal Structure of Bacillus subtilis SigW domain 4 in complexed with -35 element DNA

Summary for 6JHE
Entry DOI10.2210/pdb6jhe/pdb
DescriptorECF RNA polymerase sigma factor SigW, DNA (5'-D(P*TP*TP*GP*AP*AP*AP*CP*CP*TP*TP*T)-3'), DNA (5'-D(*AP*AP*AP*GP*GP*TP*TP*TP*CP*AP*A)-3') (3 entities in total)
Functional Keywordsprotein-dna complex, helix-turn-helix, transcription-dna complex, transcription/dna
Biological sourceBacillus subtilis (strain 168)
More
Total number of polymer chains3
Total formula weight14085.19
Authors
Kwon, E.,Devkota, S.R.,Pathak, D.,Dahal, P.,Kim, D.Y. (deposition date: 2019-02-18, release date: 2020-01-01, Last modification date: 2023-11-22)
Primary citationKwon, E.,Devkota, S.R.,Pathak, D.,Dahal, P.,Kim, D.Y.
Structural analysis of the recognition of the -35 promoter element by SigW from Bacillus subtilis.
Plos One, 14:e0221666-e0221666, 2019
Cited by
PubMed Abstract: Sigma factors are key proteins that mediate the recruitment of RNA polymerase to the promoter regions of genes, for the initiation of bacterial transcription. Multiple sigma factors in a bacterium selectively recognize their cognate promoter sequences, thereby inducing the expression of their own regulons. In this paper, we report the crystal structure of the σ4 domain of Bacillus subtilis SigW bound to the -35 promoter element. Purine-specific hydrogen bonds of the -35 promoter element with the recognition helix α9 of the σ4 domain occurs at three nucleotides of the consensus sequence (G-35, A-34, and G'-31 in G-35A-34A-33A-32C-31C-30T-29). The hydrogen bonds of the backbone with the α7 and α8 of the σ4 domain occurs at G'-30. These results elucidate the structural basis of the selective recognition of the promoter by SigW. In addition, comparison of SigW structures complexed with the -35 promoter element or with anti-sigma RsiW reveals that DNA recognition and anti-sigma factor binding of SigW are mutually exclusive.
PubMed: 31461489
DOI: 10.1371/journal.pone.0221666
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.101 Å)
Structure validation

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon