8f1j
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8f1j]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F1J FirstGlance]. <br> | <table><tr><td colspan='2'>[[8f1j]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F1J FirstGlance]. <br> | ||
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8f1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f1j OCA], [https://pdbe.org/8f1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f1j RCSB], [https://www.ebi.ac.uk/pdbsum/8f1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f1j 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=8f1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f1j OCA], [https://pdbe.org/8f1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f1j RCSB], [https://www.ebi.ac.uk/pdbsum/8f1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f1j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RPOA_ECOLI RPOA_ECOLI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.[HAMAP-Rule:MF_00059] | [https://www.uniprot.org/uniprot/RPOA_ECOLI RPOA_ECOLI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.[HAMAP-Rule:MF_00059] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Bacterial transcription initiation requires sigma factors for nucleation of the transcription bubble. The canonical housekeeping sigma factor, sigma(70), nucleates DNA melting via recognition of conserved bases of the promoter -10 motif, which are unstacked and captured in pockets of sigma(70). By contrast, the mechanism of transcription bubble nucleation and formation during the unrelated sigma(N)-mediated transcription initiation is poorly understood. Herein, we combine structural and biochemical approaches to establish that sigma(N), like sigma(70), captures a flipped, unstacked base in a pocket formed between its N-terminal region I (RI) and extra-long helix features. Strikingly, RI inserts into the nascent bubble to stabilize the nucleated bubble prior to engagement of the obligate ATPase activator. Our data suggest a general paradigm of transcription initiation that requires sigma factors to nucleate an early melted intermediate prior to productive RNA synthesis. | ||
- | + | ==See Also== | |
- | + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
SigN RNA polymerase early-melted intermediate bound to mismatch DNA fragment dhsU36mm2 (-12A)
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