5i2d
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of T. thermophilus TTHB099 class II transcription activation complex: TAP-RPo== | |
| + | <StructureSection load='5i2d' size='340' side='right'caption='[[5i2d]], [[Resolution|resolution]] 4.41Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5i2d]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] and [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I2D 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]] 4.405Å</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=5i2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i2d OCA], [https://pdbe.org/5i2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i2d RCSB], [https://www.ebi.ac.uk/pdbsum/5i2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i2d ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RPOA_THET8 RPOA_THET8] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Class II transcription activators function by binding to a DNA site overlapping a core promoter and stimulating isomerization of an initial RNA polymerase (RNAP)-promoter closed complex into a catalytically competent RNAP-promoter open complex. Here, we report a 4.4 angstrom crystal structure of an intact bacterial class II transcription activation complex. The structure comprises Thermus thermophilus transcription activator protein TTHB099 (TAP) [homolog of Escherichia coli catabolite activator protein (CAP)], T. thermophilus RNAP sigma(A) holoenzyme, a class II TAP-dependent promoter, and a ribotetranucleotide primer. The structure reveals the interactions between RNAP holoenzyme and DNA responsible for transcription initiation and reveals the interactions between TAP and RNAP holoenzyme responsible for transcription activation. The structure indicates that TAP stimulates isomerization through simple, adhesive, stabilizing protein-protein interactions with RNAP holoenzyme. | ||
| - | + | Structural basis of transcription activation.,Feng Y, Zhang Y, Ebright RH Science. 2016 Jun 10;352(6291):1330-3. doi: 10.1126/science.aaf4417. PMID:27284196<ref>PMID:27284196</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5i2d" style="background-color:#fffaf0;"></div> |
| - | [[Category: Feng | + | |
| - | [[Category: | + | ==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: Thermus thermophilus]] | ||
| + | [[Category: Thermus thermophilus HB8]] | ||
| + | [[Category: Ebright RH]] | ||
| + | [[Category: Feng Y]] | ||
| + | [[Category: Zhang Y]] | ||
Current revision
Crystal structure of T. thermophilus TTHB099 class II transcription activation complex: TAP-RPo
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