8iue

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8iue]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IUE FirstGlance]. <br>
<table><tr><td colspan='2'>[[8iue]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IUE FirstGlance]. <br>
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</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=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 4.1&#8491;</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=8iue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iue OCA], [https://pdbe.org/8iue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iue RCSB], [https://www.ebi.ac.uk/pdbsum/8iue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iue ProSAT]</span></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=8iue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iue OCA], [https://pdbe.org/8iue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iue RCSB], [https://www.ebi.ac.uk/pdbsum/8iue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iue ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[https://www.uniprot.org/uniprot/RPC1_HUMAN RPC1_HUMAN] Wiedemann-Rautenstrauch syndrome;Hypomyelination-cerebellar atrophy-hypoplasia of the corpus callosum syndrome;Hypomyelinating leukodystrophy-ataxia-hypodontia-hypomyelination syndrome;Odontoleukodystrophy;Tremor-ataxia-central hypomyelination syndrome;Hypomyelination-hypogonadotropic hypogonadism-hypodontia syndrome. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/RPAC1_HUMAN RPAC1_HUMAN] Hypomyelination-hypogonadotropic hypogonadism-hypodontia syndrome;Treacher-Collins syndrome. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/RPC1_HUMAN RPC1_HUMAN] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity). Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway.<ref>PMID:19609254</ref> <ref>PMID:19631370</ref>
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[https://www.uniprot.org/uniprot/RPAC1_HUMAN RPAC1_HUMAN] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and short non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs, respectively. POLR1C/RPAC1 is part of the polymerase core and may function as a clamp element that moves to open and close the cleft.[UniProtKB:P07703]<ref>PMID:20413673</ref> <ref>PMID:34671025</ref> <ref>PMID:34887565</ref> <ref>PMID:36271492</ref> <ref>PMID:26151409</ref>
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==See Also==
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*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
== References ==
== References ==
<references/>
<references/>

Current revision

RNA polymerase III pre-initiation complex melting complex 1

PDB ID 8iue

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