5ui5: Difference between revisions
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The | ==Crystal structure of Aquifex aeolicus sigmaN bound to promoter DNA== | ||
<StructureSection load='5ui5' size='340' side='right' caption='[[5ui5]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ui5]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UI5 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ui5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ui5 OCA], [http://pdbe.org/5ui5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ui5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ui5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ui5 ProSAT]</span></td></tr> | |||
</table> | |||
<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 5ui5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Campbell, E A]] | |||
[[Category: Darst, S A]] | |||
[[Category: Rajashankar, K]] | |||
[[Category: Helix-turn-helix dna binding motif winged helix-turn-helix dna binding motif bacterial rna polymerase sigman bacterial rna polymerase sigma54]] | |||
[[Category: Transcription-dna complex]] | |||
Revision as of 10:49, 9 March 2017
Crystal structure of Aquifex aeolicus sigmaN bound to promoter DNACrystal structure of Aquifex aeolicus sigmaN bound to promoter DNA
Structural highlights
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. References
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