7dn3: Difference between revisions

Latest revision as of 14:08, 13 August 2026

Structure of Human RNA Polymerase III elongation complex

Structural highlights

7dn3 is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.5Å
Ligands:	MG, ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

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

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]^[1] ^[2] ^[3] ^[4] ^[5]

References

↑ Canella D, Praz V, Reina JH, Cousin P, Hernandez N. Defining the RNA polymerase III transcriptome: Genome-wide localization of the RNA polymerase III transcription machinery in human cells. Genome Res. 2010 Jun;20(6):710-21. PMID:20413673 doi:10.1101/gr.101337.109
↑ Zhao D, Liu W, Chen K, Wu Z, Yang H, Xu Y. Structure of the human RNA polymerase I elongation complex. Cell Discov. 2021 Oct 20;7(1):97. PMID:34671025 doi:10.1038/s41421-021-00335-5
↑ Misiaszek AD, Girbig M, Grötsch H, Baudin F, Murciano B, Lafita A, Müller CW. Cryo-EM structures of human RNA polymerase I. Nat Struct Mol Biol. 2021 Dec;28(12):997-1008. PMID:34887565 doi:10.1038/s41594-021-00693-4
↑ Daiß JL, Pilsl M, Straub K, Bleckmann A, Höcherl M, Heiss FB, Abascal-Palacios G, Ramsay EP, Tlučková K, Mars JC, Fürtges T, Bruckmann A, Rudack T, Bernecky C, Lamour V, Panov K, Vannini A, Moss T, Engel C. The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans. Life Sci Alliance. 2022 Sep 1;5(11):e202201568. PMID:36271492 doi:10.26508/lsa.202201568
↑ Thiffault I, Wolf NI, Forget D, Guerrero K, Tran LT, Choquet K, Lavallée-Adam M, Poitras C, Brais B, Yoon G, Sztriha L, Webster RI, Timmann D, van de Warrenburg BP, Seeger J, Zimmermann A, Máté A, Goizet C, Fung E, van der Knaap MS, Fribourg S, Vanderver A, Simons C, Taft RJ, Yates JR 3rd, Coulombe B, Bernard G. Recessive mutations in POLR1C cause a leukodystrophy by impairing biogenesis of RNA polymerase III. Nat Commun. 2015 Jul 7;6:7623. PMID:26151409 doi:10.1038/ncomms8623

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Canella D, Praz V, Reina JH, Cousin P, Hernandez N. Defining the RNA polymerase III transcriptome: Genome-wide localization of the RNA polymerase III transcription machinery in human cells. Genome Res. 2010 Jun;20(6):710-21. PMID:20413673 doi:10.1101/gr.101337.109

[2] Zhao D, Liu W, Chen K, Wu Z, Yang H, Xu Y. Structure of the human RNA polymerase I elongation complex. Cell Discov. 2021 Oct 20;7(1):97. PMID:34671025 doi:10.1038/s41421-021-00335-5

[3] Misiaszek AD, Girbig M, Grötsch H, Baudin F, Murciano B, Lafita A, Müller CW. Cryo-EM structures of human RNA polymerase I. Nat Struct Mol Biol. 2021 Dec;28(12):997-1008. PMID:34887565 doi:10.1038/s41594-021-00693-4

[4] Daiß JL, Pilsl M, Straub K, Bleckmann A, Höcherl M, Heiss FB, Abascal-Palacios G, Ramsay EP, Tlučková K, Mars JC, Fürtges T, Bruckmann A, Rudack T, Bernecky C, Lamour V, Panov K, Vannini A, Moss T, Engel C. The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans. Life Sci Alliance. 2022 Sep 1;5(11):e202201568. PMID:36271492 doi:10.26508/lsa.202201568

[5] Thiffault I, Wolf NI, Forget D, Guerrero K, Tran LT, Choquet K, Lavallée-Adam M, Poitras C, Brais B, Yoon G, Sztriha L, Webster RI, Timmann D, van de Warrenburg BP, Seeger J, Zimmermann A, Máté A, Goizet C, Fung E, van der Knaap MS, Fribourg S, Vanderver A, Simons C, Taft RJ, Yates JR 3rd, Coulombe B, Bernard G. Recessive mutations in POLR1C cause a leukodystrophy by impairing biogenesis of RNA polymerase III. Nat Commun. 2015 Jul 7;6:7623. PMID:26151409 doi:10.1038/ncomms8623

[1]

[2]

[3]

[4]

[5]

@@ Line 5: / Line 5: @@
 <table><tr><td colspan='2'>[[7dn3]] 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=7DN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DN3 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]] 3.5&#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=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=MG:MAGNESIUM+ION'>MG</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=7dn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dn3 OCA], [https://pdbe.org/7dn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dn3 RCSB], [https://www.ebi.ac.uk/pdbsum/7dn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dn3 ProSAT]</span></td></tr>
 </table>
 == 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/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 ==
-[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/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>
 ==See Also==

7dn3: Difference between revisions

Latest revision as of 14:08, 13 August 2026

Structure of Human RNA Polymerase III elongation complex

Structural highlights

Disease

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools