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2K9L

Structure of the Core Binding Domain of sigma54

Summary for 2K9L
Entry DOI10.2210/pdb2k9l/pdb
Related2K9M
DescriptorRNA polymerase sigma factor RpoN (1 entity in total)
Functional Keywordsprotein, transcription
Biological sourceAquifex aeolicus
Total number of polymer chains1
Total formula weight8930.14
Authors
Hong, E.,Wemmer, D. (deposition date: 2008-10-19, release date: 2009-05-26, Last modification date: 2024-05-22)
Primary citationHong, E.,Doucleff, M.,Wemmer, D.E.
Structure of the RNA polymerase core-binding domain of sigma(54) reveals a likely conformational fracture point
J.Mol.Biol., 390:70-82, 2009
Cited by
PubMed Abstract: Transcription initiation by bacterial sigma(54)-RNA polymerase requires a conformational change of the holopolymerase-DNA complex, driven by an enhancer-binding protein. Although structures of the core polymerase and the more common sigma(70) factor have been determined, little is known about the structure of the sigma(54) variant. We report here the structure of an Aquifex aeolicus sigma(54) domain (residues 69-198), which binds core RNA polymerase. The structure is composed of two distinct subdomains held together by a small, conserved hydrophobic interface that appears to act as a fracture point in the structure. The N-terminal, four-helical subdomain has a negative surface and conserved residues that likely contact the core polymerase, while the C-terminal, three-helical bundle has a strongly positive patch that could contact DNA. Sequence conservation indicates that these structural features are conserved and are important for the role of sigma(54) in the polymerase complex.
PubMed: 19426742
DOI: 10.1016/j.jmb.2009.04.070
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

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