2O8K

NMR Structure of the Sigma-54 RpoN Domain Bound to the-24 Promoter Element

Summary for 2O8K

• Entry DOI: 10.2210/pdb2o8k/pdb
• NMR Information: BMRB: 15083
• Descriptor: 5'-D(*TP*TP*TP*TP*GP*GP*CP*AP*CP*GP*TP*TP*TP*C)-3', 5'-D(*GP*AP*AP*AP*CP*GP*TP*GP*CP*CP*AP*AP*AP*A)-3', RNA polymerase sigma factor RpoN (3 entities in total)
• Functional Keywords: protein-dna complex, helix-turn-helix, transcription factor, sigma-54, rna polymerase, transcription-dna complex, transcription/dna
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 3
• Total formula weight: 16048.41

Authors

Doucleff, M.,Pelton, J.G.,Lee, P.S.,Wemmer, D.E. (deposition date: 2006-12-12, release date: 2007-07-17, Last modification date: 2023-12-27)

Primary citation

Doucleff, M.,Pelton, J.G.,Lee, P.S.,Nixon, B.T.,Wemmer, D.E.
Structural basis of DNA recognition by the alternative sigma-factor, sigma54.
J.Mol.Biol., 369:1070-1078, 2007

PubMed Abstract: The sigma subunit of bacterial RNA polymerase (RNAP) regulates gene expression by directing RNAP to specific promoters. Unlike sigma(70)-type proteins, the alternative sigma factor, sigma(54), requires interaction with an ATPase to open DNA. We present the solution structure of the C-terminal domain of sigma(54) bound to the -24 promoter element, in which the conserved RpoN box motif inserts into the major groove of the DNA. This structure elucidates the basis for sequence specific recognition of the -24 element, orients sigma(54) on the promoter, and suggests how the C-terminal domain of sigma(54) interacts with RNAP.

PubMed: 17481658
DOI: 10.1016/j.jmb.2007.04.019

Experimental method

SOLUTION NMR