2max: Difference between revisions
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==NMR structure of the RNA polymerase alpha subunit C-terminal domain from Helicobacter pylori== | ==NMR structure of the RNA polymerase alpha subunit C-terminal domain from Helicobacter pylori== | ||
<StructureSection load='2max' size='340' side='right'caption='[[2max | <StructureSection load='2max' size='340' side='right'caption='[[2max]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2max]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2max]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_J99 Helicobacter pylori J99]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAX FirstGlance]. <br> | ||
</td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2max OCA], [https://pdbe.org/2max PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2max RCSB], [https://www.ebi.ac.uk/pdbsum/2max PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2max ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2max OCA], [https://pdbe.org/2max PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2max RCSB], [https://www.ebi.ac.uk/pdbsum/2max PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2max ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RPOA_HELPJ RPOA_HELPJ] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Helicobacter pylori J99]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Borin | [[Category: Borin BN]] | ||
[[Category: Krezel | [[Category: Krezel AM]] | ||
Revision as of 09:30, 2 March 2023
NMR structure of the RNA polymerase alpha subunit C-terminal domain from Helicobacter pyloriNMR structure of the RNA polymerase alpha subunit C-terminal domain from Helicobacter pylori
Structural highlights
FunctionRPOA_HELPJ DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity). Publication Abstract from PubMedBacterial 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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