2max | pdb_00002max

NMR structure of the RNA polymerase alpha subunit C-terminal domain from Helicobacter pylori

spinqualitylabelsall models 2max, 15 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2max is a 1 chain structure with sequence from Campylobacter pylori j99. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: jhp_1213, rpoA (Campylobacter pylori J99) Activity: DNA-directed RNA polymerase, with EC number 2.7.7.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [RPOA_HELPJ] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity). Publication Abstract from PubMed Bacterial RNA polymerase is a large, multi-subunit enzyme responsible for transcription of genomic information. The C-terminal domain of the alpha subunit of RNA polymerase (alphaCTD) functions as a DNA and protein recognition element localizing the polymerase on certain promoter sequences and is essential in all bacteria. Although alphaCTD is part of RNA polymerase, it is thought to have once been a separate transcription factor, and its primary role is the recruitment of RNA polymerase to various promoters. Despite the conservation of the subunits of RNA polymerase among bacteria, the mechanisms of regulation of transcription vary significantly. We have determined the tertiary structure of Helicobacter pylori alphaCTD. It is larger than other structurally determined alphaCTDs due to an extra, highly amphipathic helix near the C-terminal end. Residues within this helix are highly conserved among varepsilon-proteobacteria. The surface of the domain that binds A/T rich DNA sequences is conserved and showed binding to DNA similar to alphaCTDs of other bacteria. Using several NikR dependent promoter sequences, we observed cooperative binding of H. pylori alphaCTD to NikR:DNA complexes. We also produced alphaCTD lacking the 19 C-terminal residues, which showed greatly decreased stability, but maintained the core domain structure and binding affinity to NikR:DNA at low temperatures. The modeling of H. pylori alphaCTD into the context of transcriptional complexes suggests that the additional amphipathic helix mediates interactions with transcriptional regulators. Helicobacter pylori RNA polymerase alpha-subunit C-terminal domain shows features unique to varepsilon-proteobacteria and binds NikR/DNA complexes.,Borin BN, Tang W, Krezel AM Protein Sci. 2014 Jan 17. doi: 10.1002/pro.2427. PMID:24442709 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RNA polymerase Temp1

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