7d59: Difference between revisions

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<table><tr><td colspan='2'>[[7d59]] 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=7D59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D59 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7d59]] 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=7D59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D59 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7d59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d59 OCA], [https://pdbe.org/7d59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d59 RCSB], [https://www.ebi.ac.uk/pdbsum/7d59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d59 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=7d59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d59 OCA], [https://pdbe.org/7d59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d59 RCSB], [https://www.ebi.ac.uk/pdbsum/7d59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d59 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[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.
[https://www.uniprot.org/uniprot/RPC1_HUMAN RPC1_HUMAN] Wiedemann-Rautenstrauch syndrome;Hypomyelination-hypogonadotropic hypogonadism-hypodontia syndrome;Hypomyelinating leukodystrophy-ataxia-hypodontia-hypomyelination syndrome;Tremor-ataxia-central hypomyelination syndrome;Odontoleukodystrophy;Hypomyelination-cerebellar atrophy-hypoplasia of the corpus callosum 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 ==
[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>  
[https://www.uniprot.org/uniprot/RPC1_HUMAN RPC1_HUMAN] Catalytic core component of RNA polymerase III (Pol III), a DNA-dependent RNA polymerase which synthesizes small non-coding RNAs using the four ribonucleoside triphosphates as substrates. Synthesizes 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci (PubMed:19609254, PubMed:19631370, PubMed:20413673, PubMed:33335104, PubMed:33558764, PubMed:33558766, PubMed:34675218, PubMed:35637192, PubMed:9331371). Pol III-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol III is recruited to DNA promoters type I, II or III with the help of general transcription factors and other specific initiation factors. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (PubMed:20413673, PubMed:33335104, PubMed:33558764, PubMed:33558766, PubMed:33674783, PubMed:34675218). Forms Pol III active center together with the second largest subunit POLR3B/RPC2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR3A/RPC1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR3B/RPC2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate (PubMed:19609254, PubMed:20413673, PubMed:33335104, PubMed:33558764, PubMed:33674783, PubMed:34675218, PubMed:9331371). Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as a 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> <ref>PMID:20413673</ref> <ref>PMID:33335104</ref> <ref>PMID:33558764</ref> <ref>PMID:33558766</ref> <ref>PMID:33674783</ref> <ref>PMID:34675218</ref> <ref>PMID:35637192</ref> <ref>PMID:9331371</ref>  


==See Also==
==See Also==