5UI5

Crystal structure of Aquifex aeolicus sigmaN bound to promoter DNA

Summary for 5UI5

• Entry DOI: 10.2210/pdb5ui5/pdb
• Descriptor: DNA (31-MER), DNA (30-MER), RNA polymerase sigma factor RpoN, ... (4 entities in total)
• Functional Keywords: helix-turn-helix dna binding motif winged helix-turn-helix dna binding motif bacterial rna polymerase sigman bacterial rna polymerase sigma54, transcription-dna complex, transcription/dna
• Biological source: Aquifex aeolicus (strain VF5); More
• Total number of polymer chains: 6
• Total formula weight: 118877.68

Authors

Darst, S.A.,Campbell, E.A.,Rajashankar, K. (deposition date: 2017-01-12, release date: 2017-02-22, Last modification date: 2024-03-06)

Primary citation

Campbell, E.A.,Kamath, S.,Rajashankar, K.R.,Wu, M.,Darst, S.A.
Crystal structure of Aquifex aeolicus sigma (N) bound to promoter DNA and the structure of sigma (N)-holoenzyme.
Proc. Natl. Acad. Sci. U.S.A., 114:E1805-E1814, 2017

PubMed Abstract: The bacterial σ factors confer promoter specificity to the RNA polymerase (RNAP). One alternative σ factor, σ, is unique in its structure and functional mechanism, forming transcriptionally inactive promoter complexes that require activation by specialized AAA ATPases. We report a 3.4-Å resolution X-ray crystal structure of a σ fragment in complex with its cognate promoter DNA, revealing the molecular details of promoter recognition by σ The structure allowed us to build and refine an improved σ-holoenzyme model based on previously published 3.8-Å resolution X-ray data. The improved σ-holoenzyme model reveals a conserved interdomain interface within σ that, when disrupted by mutations, leads to transcription activity without activator intervention (so-called bypass mutants). Thus, the structure and stability of this interdomain interface are crucial for the role of σ in blocking transcription activity and in maintaining the activator sensitivity of σ.

PubMed: 28223493
DOI: 10.1073/pnas.1619464114

Experimental method

X-RAY DIFFRACTION (3.4 Å)