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==Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin== | ==Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin== | ||
<StructureSection load='1zyr' size='340' side='right' caption='[[1zyr]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1zyr' size='340' side='right'caption='[[1zyr]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1zyr]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1zyr]] 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=1ZYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZYR 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]] 3Å</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=1zyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zyr OCA], [https://pdbe.org/1zyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zyr RCSB], [https://www.ebi.ac.uk/pdbsum/1zyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zyr ProSAT]</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/zy/1zyr_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zy/1zyr_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 31: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[RNA polymerase|RNA polymerase]] | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Arnold | [[Category: Arnold E]] | ||
[[Category: Birktoft | [[Category: Birktoft JJ]] | ||
[[Category: Borukhov | [[Category: Borukhov S]] | ||
[[Category: Clark | [[Category: Clark AD]] | ||
[[Category: Dharia | [[Category: Dharia C]] | ||
[[Category: Ebright | [[Category: Ebright RH]] | ||
[[Category: Hudson | [[Category: Hudson B]] | ||
[[Category: Ismail | [[Category: Ismail S]] | ||
[[Category: Laptenko | [[Category: Laptenko O]] | ||
[[Category: Lee | [[Category: Lee J]] | ||
[[Category: Leroy | [[Category: Leroy O]] | ||
[[Category: Mukhopadhyay | [[Category: Mukhopadhyay J]] | ||
[[Category: Napoli | [[Category: Napoli A]] | ||
[[Category: Sarafianos | [[Category: Sarafianos SG]] | ||
[[Category: Sineva | [[Category: Sineva E]] | ||
[[Category: Tuske | [[Category: Tuske S]] | ||
[[Category: Wang | [[Category: Wang X]] | ||
Latest revision as of 03:45, 21 November 2024
Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydiginStructure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin
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 PubMedWe define the target, mechanism, and structural basis of inhibition of bacterial RNA polymerase (RNAP) by the tetramic acid antibiotic streptolydigin (Stl). Stl binds to a site adjacent to but not overlapping the RNAP active center and stabilizes an RNAP-active-center conformational state with a straight-bridge helix. The results provide direct support for the proposals that alternative straight-bridge-helix and bent-bridge-helix RNAP-active-center conformations exist and that cycling between straight-bridge-helix and bent-bridge-helix RNAP-active-center conformations is required for RNAP function. The results set bounds on models for RNAP function and suggest strategies for design of novel antibacterial agents. Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation.,Tuske S, Sarafianos SG, Wang X, Hudson B, Sineva E, Mukhopadhyay J, Birktoft JJ, Leroy O, Ismail S, Clark AD Jr, Dharia C, Napoli A, Laptenko O, Lee J, Borukhov S, Ebright RH, Arnold E Cell. 2005 Aug 26;122(4):541-52. PMID:16122422[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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