2ahq

Solution Structure of the C-terminal RpoN Domain of Sigma-54 from Aquifex aeolicus

spinqualitylabelsall models 2ahq Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ahq is a 1 chain structure with sequence from Aquifex aeolicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O66858_AQUAE 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 The "sigma" subunit of prokaryotic RNA polymerase allows gene-specific transcription initiation. Two sigma families have been identified, sigma70 and sigma54, which use distinct mechanisms to initiate transcription and share no detectable sequence homology. Although the sigma70-type factors have been well characterized structurally by x-ray crystallography, no high resolution structural information is available for the sigma54-type factors. Here we present the NMR-derived structure of the C-terminal domain of sigma54 from Aquifex aeolicus. This domain (Thr-323 to Gly-389), which contains the highly conserved RpoN box sequence, consists of a poorly structured N-terminal tail followed by a three-helix bundle, which is surprisingly similar to domains of the sigma70-type proteins. Residues of the RpoN box, which have previously been shown to be critical for DNA binding, form the second helix of an unpredicted helix-turn-helix motif. The homology of this structure with other DNA-binding proteins, combined with previous biochemical data, suggests how the C-terminal domain of sigma54 binds to DNA. The C-terminal RpoN domain of sigma54 forms an unpredicted helix-turn-helix motif similar to domains of sigma70.,Doucleff M, Malak LT, Pelton JG, Wemmer DE J Biol Chem. 2005 Dec 16;280(50):41530-6. Epub 2005 Oct 6. PMID:16210314 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sigma factor 3D structures

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