2k9m | pdb_00002k9m

Structure of the Core Binding Domain of sigma54

spinqualitylabelsall models 2k9m, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k9m is a 1 chain structure with sequence from "aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2k9l Gene: rpoN ("Aquifex aeolicus" Huber and Stetter 2001) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of the RNA polymerase core-binding domain of sigma(54) reveals a likely conformational fracture point.,Hong E, Doucleff M, Wemmer DE J Mol Biol. 2009 Jul 3;390(1):70-82. Epub 2009 May 5. PMID:19426742 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sigma factor

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