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[[Image:1i6v.gif|left|200px]]
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{{STRUCTURE_1i6v|  PDB=1i6v  |  SCENE=  }}
'''THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX'''


==THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX==
<StructureSection load='1i6v' size='340' side='right'caption='[[1i6v]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1i6v]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I6V 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]] 3.3&#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=RFP:RIFAMPICIN'>RFP</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=1i6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6v OCA], [https://pdbe.org/1i6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i6v RCSB], [https://www.ebi.ac.uk/pdbsum/1i6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i6v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RPOA_THEAQ RPOA_THEAQ]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i6/1i6v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i6v ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rifampicin (Rif) is one of the most potent and broad spectrum antibiotics against bacterial pathogens and is a key component of anti-tuberculosis therapy, stemming from its inhibition of the bacterial RNA polymerase (RNAP). We determined the crystal structure of Thermus aquaticus core RNAP complexed with Rif. The inhibitor binds in a pocket of the RNAP beta subunit deep within the DNA/RNA channel, but more than 12 A away from the active site. The structure, combined with biochemical results, explains the effects of Rif on RNAP function and indicates that the inhibitor acts by directly blocking the path of the elongating RNA when the transcript becomes 2 to 3 nt in length.


==Overview==
Structural mechanism for rifampicin inhibition of bacterial rna polymerase.,Campbell EA, Korzheva N, Mustaev A, Murakami K, Nair S, Goldfarb A, Darst SA Cell. 2001 Mar 23;104(6):901-12. PMID:11290327<ref>PMID:11290327</ref>
Rifampicin (Rif) is one of the most potent and broad spectrum antibiotics against bacterial pathogens and is a key component of anti-tuberculosis therapy, stemming from its inhibition of the bacterial RNA polymerase (RNAP). We determined the crystal structure of Thermus aquaticus core RNAP complexed with Rif. The inhibitor binds in a pocket of the RNAP beta subunit deep within the DNA/RNA channel, but more than 12 A away from the active site. The structure, combined with biochemical results, explains the effects of Rif on RNAP function and indicates that the inhibitor acts by directly blocking the path of the elongating RNA when the transcript becomes 2 to 3 nt in length.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1I6V is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6V OCA].
</div>
<div class="pdbe-citations 1i6v" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural mechanism for rifampicin inhibition of bacterial rna polymerase., Campbell EA, Korzheva N, Mustaev A, Murakami K, Nair S, Goldfarb A, Darst SA, Cell. 2001 Mar 23;104(6):901-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11290327 11290327]
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
[[Category: DNA-directed RNA polymerase]]
== References ==
[[Category: Protein complex]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
[[Category: Campbell, E A.]]
[[Category: Campbell EA]]
[[Category: Darst, S A.]]
[[Category: Darst SA]]
[[Category: Goldfarb, A.]]
[[Category: Goldfarb A]]
[[Category: Korzheva, N.]]
[[Category: Korzheva N]]
[[Category: Murakami, K.]]
[[Category: Murakami K]]
[[Category: Mustaev, A.]]
[[Category: Mustaev A]]
[[Category: 3d- structure]]
[[Category: Dna-directed rna polymerase]]
[[Category: Transcription]]
[[Category: Transferase]]
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