4xls: Difference between revisions

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New page: '''Unreleased structure''' The entry 4xls is ON HOLD Authors: Bae, B., Darst, S.A. Description: Crystal structure of T.aquaticus transcription initiation complex with CarD containing u...
 
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'''Unreleased structure'''


The entry 4xls is ON HOLD
==Crystal structure of T. aquaticus transcription initiation complex with CarD containing upstream fork promoter.==
<StructureSection load='4xls' size='340' side='right'caption='[[4xls]], [[Resolution|resolution]] 4.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xls]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus], [https://en.wikipedia.org/wiki/Thermus_thermophilus_JL-18 Thermus thermophilus JL-18] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XLS 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]] 4.01&#8491;</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=4xls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xls OCA], [https://pdbe.org/4xls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xls RCSB], [https://www.ebi.ac.uk/pdbsum/4xls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xls ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RPOA_THEAQ RPOA_THEAQ]
<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.


Authors: Bae, B., Darst, S.A.
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>


Description: Crystal structure of T.aquaticus transcription initiation complex with CarD containing upstream fork promoter.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Darst, S.A]]
<div class="pdbe-citations 4xls" style="background-color:#fffaf0;"></div>
[[Category: Bae, B]]
 
==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
*[[Sigma factor 3D structures|Sigma factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Thermus aquaticus]]
[[Category: Thermus thermophilus JL-18]]
[[Category: Bae B]]
[[Category: Darst SA]]

Latest revision as of 13:32, 30 October 2024

Crystal structure of T. aquaticus transcription initiation complex with CarD containing upstream fork promoter.Crystal structure of T. aquaticus transcription initiation complex with CarD containing upstream fork promoter.

Structural highlights

4xls is a 18 chain structure with sequence from Thermus aquaticus, Thermus thermophilus JL-18 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.01Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPOA_THEAQ

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Bae B, Chen J, Davis E, Leon K, Darst SA, Campbell EA. CarD uses a minor groove wedge mechanism to stabilize the RNA polymerase open promoter complex. Elife. 2015 Sep 8;4. doi: 10.7554/eLife.08505. PMID:26349034 doi:http://dx.doi.org/10.7554/eLife.08505

4xls, resolution 4.01Å

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