5ui8: Difference between revisions
New page: '''Unreleased structure''' The entry 5ui8 is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==structure of sigmaN-holoenzyme== | ||
<StructureSection load='5ui8' size='340' side='right'caption='[[5ui8]], [[Resolution|resolution]] 3.76Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ui8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7], [https://en.wikipedia.org/wiki/Escherichia_coli_S88 Escherichia coli S88] and [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UI8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.76Å</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=5ui8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ui8 OCA], [https://pdbe.org/5ui8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ui8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ui8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ui8 ProSAT]</span></td></tr> | |||
</table> | |||
== 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] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bacterial sigma factors confer promoter specificity to the RNA polymerase (RNAP). One alternative sigma factor, sigmaN, is unique in its structure and functional mechanism, forming transcriptionally inactive promoter complexes that require activation by specialized AAA+ ATPases. We report a 3.4-A resolution X-ray crystal structure of a sigmaN fragment in complex with its cognate promoter DNA, revealing the molecular details of promoter recognition by sigmaN The structure allowed us to build and refine an improved sigmaN-holoenzyme model based on previously published 3.8-A resolution X-ray data. The improved sigmaN-holoenzyme model reveals a conserved interdomain interface within sigmaN that, when disrupted by mutations, leads to transcription activity without activator intervention (so-called bypass mutants). Thus, the structure and stability of this interdomain interface are crucial for the role of sigmaN in blocking transcription activity and in maintaining the activator sensitivity of sigmaN. | |||
Crystal structure of Aquifex aeolicus sigmaN bound to promoter DNA and the structure of sigmaN-holoenzyme.,Campbell EA, Kamath S, Rajashankar KR, Wu M, Darst SA Proc Natl Acad Sci U S A. 2017 Feb 21. pii: 201619464. doi:, 10.1073/pnas.1619464114. PMID:28223493<ref>PMID:28223493</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5ui8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
*[[Sigma factor 3D structures|Sigma factor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli O157:H7]] | |||
[[Category: Escherichia coli S88]] | |||
[[Category: Klebsiella pneumoniae]] | |||
[[Category: Large Structures]] | |||
[[Category: Campbell EA]] | |||
[[Category: Darst SA]] | |||
Latest revision as of 16:27, 4 October 2023
structure of sigmaN-holoenzymestructure of sigmaN-holoenzyme
Structural highlights
FunctionRPOA_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] Publication Abstract from PubMedThe bacterial sigma factors confer promoter specificity to the RNA polymerase (RNAP). One alternative sigma factor, sigmaN, is unique in its structure and functional mechanism, forming transcriptionally inactive promoter complexes that require activation by specialized AAA+ ATPases. We report a 3.4-A resolution X-ray crystal structure of a sigmaN fragment in complex with its cognate promoter DNA, revealing the molecular details of promoter recognition by sigmaN The structure allowed us to build and refine an improved sigmaN-holoenzyme model based on previously published 3.8-A resolution X-ray data. The improved sigmaN-holoenzyme model reveals a conserved interdomain interface within sigmaN that, when disrupted by mutations, leads to transcription activity without activator intervention (so-called bypass mutants). Thus, the structure and stability of this interdomain interface are crucial for the role of sigmaN in blocking transcription activity and in maintaining the activator sensitivity of sigmaN. Crystal structure of Aquifex aeolicus sigmaN bound to promoter DNA and the structure of sigmaN-holoenzyme.,Campbell EA, Kamath S, Rajashankar KR, Wu M, Darst SA Proc Natl Acad Sci U S A. 2017 Feb 21. pii: 201619464. doi:, 10.1073/pnas.1619464114. PMID:28223493[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||