2K9L
Structure of the Core Binding Domain of sigma54
Summary for 2K9L
Entry DOI | 10.2210/pdb2k9l/pdb |
Related | 2K9M |
Descriptor | RNA polymerase sigma factor RpoN (1 entity in total) |
Functional Keywords | protein, transcription |
Biological source | Aquifex aeolicus |
Total number of polymer chains | 1 |
Total formula weight | 8930.14 |
Authors | Hong, E.,Wemmer, D. (deposition date: 2008-10-19, release date: 2009-05-26, Last modification date: 2024-05-22) |
Primary citation | Hong, 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: 19426742DOI: 10.1016/j.jmb.2009.04.070 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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