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==Crystal structure of the T. thermophilus RNA polymerase holoenzyme in complex with antibiotic sterptolydigin== | ==Crystal structure of the T. thermophilus RNA polymerase holoenzyme in complex with antibiotic sterptolydigin== | ||
<StructureSection load='2a6h' size='340' side='right' caption='[[2a6h]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2a6h' size='340' side='right'caption='[[2a6h]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2a6h]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2a6h]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A6H FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id=' | <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=STD:STREPTOLYDIGIN'>STD</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=2a6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6h OCA], [https://pdbe.org/2a6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a6h RCSB], [https://www.ebi.ac.uk/pdbsum/2a6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6h ProSAT], [https://www.topsan.org/Proteins/RSGI/2a6h TOPSAN]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/2a6h_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/2a6h_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 31: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[RNA polymerase|RNA polymerase]] | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
*[[Sigma factor|Sigma factor]] | *[[Sigma factor 3D structures|Sigma factor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Igarashi | [[Category: Igarashi N]] | ||
[[Category: Matsugaki | [[Category: Matsugaki N]] | ||
[[Category: Nikiforov | [[Category: Nikiforov V]] | ||
[[Category: Perederina | [[Category: Perederina A]] | ||
[[Category: Savkina M]] | |||
[[Category: Savkina | [[Category: Severinov K]] | ||
[[Category: Severinov | [[Category: Tahirov TH]] | ||
[[Category: Tahirov | [[Category: Temiakov D]] | ||
[[Category: Temiakov | [[Category: Vassylyev DG]] | ||
[[Category: Vassylyev | [[Category: Vassylyeva MN]] | ||
[[Category: Vassylyeva | [[Category: Wakatsuki S]] | ||
[[Category: Wakatsuki | [[Category: Zenkin N]] | ||
[[Category: Zenkin | [[Category: Zorov S]] | ||
[[Category: Zorov | |||
Latest revision as of 10:19, 23 August 2023
Crystal structure of the T. thermophilus RNA polymerase holoenzyme in complex with antibiotic sterptolydiginCrystal structure of the T. thermophilus RNA polymerase holoenzyme in complex with antibiotic sterptolydigin
Structural highlights
FunctionRPOA_THET8 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStreptolydigin (Stl) is a potent inhibitor of bacterial RNA polymerases (RNAPs). The 2.4 A resolution structure of the Thermus thermophilus RNAP-Stl complex showed that, in full agreement with the available genetic data, the inhibitor binding site is located 20 A away from the RNAP active site and encompasses the bridge helix and the trigger loop, two elements that are considered to be crucial for RNAP catalytic center function. Structure-based biochemical experiments revealed additional determinants of Stl binding and demonstrated that Stl does not affect NTP substrate binding, DNA translocation, and phosphodiester bond formation. The RNAP-Stl complex structure, its comparison with the closely related substrate bound eukaryotic transcription elongation complexes, and biochemical analysis suggest an inhibitory mechanism in which Stl stabilizes catalytically inactive (preinsertion) substrate bound transcription intermediate, thereby blocking structural isomerization of RNAP to an active configuration. The results provide a basis for a design of new antibiotics utilizing the Stl-like mechanism. Structural basis of transcription inhibition by antibiotic streptolydigin.,Temiakov D, Zenkin N, Vassylyeva MN, Perederina A, Tahirov TH, Kashkina E, Savkina M, Zorov S, Nikiforov V, Igarashi N, Matsugaki N, Wakatsuki S, Severinov K, Vassylyev DG Mol Cell. 2005 Sep 2;19(5):655-66. PMID:16167380[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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