6exv

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==Structure of mammalian RNA polymerase II elongation complex inhibited by Alpha-amanitin==
==Structure of mammalian RNA polymerase II elongation complex inhibited by Alpha-amanitin==
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<StructureSection load='6exv' size='340' side='right' caption='[[6exv]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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<SX load='6exv' size='340' side='right' viewer='molstar' caption='[[6exv]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6exv]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Amanita_phalloides Amanita phalloides], [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EXV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6exv]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EXV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=ILX:4,5-DIHYDROXYISOLEUCINE'>ILX</scene>, <scene name='pdbligand=TRX:6-HYDROXYTRYPTOPHAN'>TRX</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=ILX:4,5-DIHYDROXYISOLEUCINE'>ILX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRX:6-HYDROXYTRYPTOPHAN'>TRX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6exv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6exv OCA], [https://pdbe.org/6exv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6exv RCSB], [https://www.ebi.ac.uk/pdbsum/6exv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6exv ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6exv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6exv OCA], [http://pdbe.org/6exv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6exv RCSB], [http://www.ebi.ac.uk/pdbsum/6exv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6exv ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/I3LGP4_PIG I3LGP4_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU363031] [[http://www.uniprot.org/uniprot/I3LJR4_PIG I3LJR4_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279] [[http://www.uniprot.org/uniprot/RPB9_PIG RPB9_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity). [[http://www.uniprot.org/uniprot/I3LCB2_PIG I3LCB2_PIG]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.[PIRNR:PIRNR000779]
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[https://www.uniprot.org/uniprot/I3LJR4_PIG I3LJR4_PIG] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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RNA polymerase II (Pol II) is the central enzyme that transcribes eukaryotic protein-coding genes to produce mRNA. The mushroom toxin alpha-amanitin binds Pol II and inhibits transcription at the step of RNA chain elongation. Pol II from yeast binds alpha-amanitin with micromolar affinity, whereas metazoan Pol II enzymes exhibit nanomolar affinities. Here, we present the high-resolution cryo-EM structure of alpha-amanitin bound to and inhibited by its natural target, the mammalian Pol II elongation complex. The structure revealed that the toxin is located in a pocket previously identified in yeast Pol II, but forms additional contacts with metazoan-specific residues, which explain why its affinity to mammalian Pol II is ~3000 times higher than for yeast Pol II. Our work provides the structural basis for the inhibition of mammalian Pol II by the natural toxin alpha-amanitin and highlights that cryo-EM is well suited to studying interactions of a small molecule with its macromolecular target.
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Cryo-EM structure of a mammalian RNA polymerase II elongation complex inhibited by alpha-amanitin.,Liu X, Farnung L, Wigge C, Cramer P J Biol Chem. 2018 Mar 17. pii: RA118.002545. doi: 10.1074/jbc.RA118.002545. PMID:29550768<ref>PMID:29550768</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6exv" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Amanita phalloides]]
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[[Category: Large Structures]]
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[[Category: DNA-directed RNA polymerase]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Cramer, P]]
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[[Category: Cramer P]]
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[[Category: Farnung, L]]
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[[Category: Farnung L]]
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[[Category: Liu, X]]
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[[Category: Liu X]]
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[[Category: Wigge, C]]
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[[Category: Wigge C]]
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[[Category: Active site]]
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[[Category: Elongation]]
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[[Category: Inhibitor]]
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[[Category: Transcription]]
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Current revision

Structure of mammalian RNA polymerase II elongation complex inhibited by Alpha-amanitin

6exv, resolution 3.60Å

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