8iue: Difference between revisions

Latest revision as of 07:40, 3 July 2024

RNA polymerase III pre-initiation complex melting complex 1

Structural highlights

8iue 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 4.1Å
Ligands:	MG, SF4, 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

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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

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[5]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8iue is ON HOLD
+==RNA polymerase III pre-initiation complex melting complex 1==
+<StructureSection load='8iue' size='340' side='right'caption='[[8iue]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
+== 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>
+</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>
+<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>
+</table>
+== Disease ==
+[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/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>
-Authors: Hou, H., Jin, Q., Ren, Y., Wang, Q., Xu, Y.
+==See Also==
+*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
-Description: human RNA polymerase III pre-initiation complex closed DNA 1
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Wang, Q]]
+__TOC__
-[[Category: Hou, H]]
+</StructureSection>
-[[Category: Ren, Y]]
+[[Category: Homo sapiens]]
-[[Category: Jin, Q]]
+[[Category: Large Structures]]
-[[Category: Xu, Y]]
+[[Category: Hou H]]
+[[Category: Jin Q]]
+[[Category: Ren Y]]
+[[Category: Wang Q]]
+[[Category: Xu Y]]

8iue: Difference between revisions

Latest revision as of 07:40, 3 July 2024

RNA polymerase III pre-initiation complex melting complex 1

Structural highlights

Disease

Function

See Also

References

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