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''' | ==Crystal structure of Thermus thermophilus CarD in complex with the Thermus aquaticus RNA polymerase beta1 domain== | ||
<StructureSection load='4xax' size='340' side='right' caption='[[4xax]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xax]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XAX FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></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=4xax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xax OCA], [http://pdbe.org/4xax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xax RCSB], [http://www.ebi.ac.uk/pdbsum/4xax PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A key point to regulate gene expression is at transcription initiation, and activators play a major role. CarD, an essential activator in Mycobacterium tuberculosis, is found in many bacteria, including Thermus species, but absent in Escherichia coli. To delineate the molecular mechanism of CarD, we determined crystal structures of Thermus transcription initiation complexes containing CarD. The structures show CarD interacts with the unique DNA topology presented by the upstream double-stranded/single-stranded DNA junction of the transcription bubble. We confirm that our structures correspond to functional activation complexes, and extend our understanding of the role of a conserved CarD Trp residue that serves as a minor groove wedge, preventing collapse of the transcription bubble to stabilize the transcription initiation complex. Unlike E. coli RNAP, many bacterial RNAPs form unstable promoter complexes, explaining the need for CarD. | |||
CarD uses a minor groove wedge mechanism to stabilize the RNA polymerase open promoter complex.,Bae B, Chen J, Davis E, Leon K, Darst SA, Campbell EA Elife. 2015 Sep 8;4. doi: 10.7554/eLife.08505. PMID:26349034<ref>PMID:26349034</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4xax" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: DNA-directed RNA polymerase]] | |||
[[Category: Bae, B]] | |||
[[Category: Campbell, E A]] | |||
[[Category: Chen, J]] | [[Category: Chen, J]] | ||
[[Category: | [[Category: Darst, S A]] | ||
[[Category: | [[Category: Transcription regulator]] | ||
Revision as of 10:44, 30 September 2015
Crystal structure of Thermus thermophilus CarD in complex with the Thermus aquaticus RNA polymerase beta1 domainCrystal structure of Thermus thermophilus CarD in complex with the Thermus aquaticus RNA polymerase beta1 domain
Structural highlights
Publication Abstract from PubMedA key point to regulate gene expression is at transcription initiation, and activators play a major role. CarD, an essential activator in Mycobacterium tuberculosis, is found in many bacteria, including Thermus species, but absent in Escherichia coli. To delineate the molecular mechanism of CarD, we determined crystal structures of Thermus transcription initiation complexes containing CarD. The structures show CarD interacts with the unique DNA topology presented by the upstream double-stranded/single-stranded DNA junction of the transcription bubble. We confirm that our structures correspond to functional activation complexes, and extend our understanding of the role of a conserved CarD Trp residue that serves as a minor groove wedge, preventing collapse of the transcription bubble to stabilize the transcription initiation complex. Unlike E. coli RNAP, many bacterial RNAPs form unstable promoter complexes, explaining the need for CarD. CarD uses a minor groove wedge mechanism to stabilize the RNA polymerase open promoter complex.,Bae B, Chen J, Davis E, Leon K, Darst SA, Campbell EA Elife. 2015 Sep 8;4. doi: 10.7554/eLife.08505. PMID:26349034[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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