8d0b

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8d0b]] is a 8 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=8D0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D0B FirstGlance]. <br>
<table><tr><td colspan='2'>[[8d0b]] is a 8 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=8D0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D0B FirstGlance]. <br>
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</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=8d0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d0b OCA], [https://pdbe.org/8d0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d0b RCSB], [https://www.ebi.ac.uk/pdbsum/8d0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d0b ProSAT]</span></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]] 3.43&#8491;</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=8d0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d0b OCA], [https://pdbe.org/8d0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d0b RCSB], [https://www.ebi.ac.uk/pdbsum/8d0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d0b ProSAT]</span></td></tr>
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</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/CTC1_HUMAN CTC1_HUMAN]] Coats plus syndrome;Dyskeratosis congenita. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/CTC1_HUMAN CTC1_HUMAN] Coats plus syndrome;Dyskeratosis congenita. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CTC1_HUMAN CTC1_HUMAN]] Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha (PubMed:22763445). The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins (PubMed:25483097). Involved in telomere maintenance (PubMed:19854131, PubMed:22863775). Involved in genome stability (PubMed:22863775). May be in involved in telomeric C-strand fill-in during late S/G2 phase (By similarity).[UniProtKB:Q5SUQ9]<ref>PMID:19854130</ref> <ref>PMID:19854131</ref> <ref>PMID:22763445</ref> <ref>PMID:22863775</ref> <ref>PMID:25483097</ref>
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[https://www.uniprot.org/uniprot/CTC1_HUMAN CTC1_HUMAN] Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha (PubMed:22763445). The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins (PubMed:25483097). Involved in telomere maintenance (PubMed:19854131, PubMed:22863775). Involved in genome stability (PubMed:22863775). May be in involved in telomeric C-strand fill-in during late S/G2 phase (By similarity).[UniProtKB:Q5SUQ9]<ref>PMID:19854130</ref> <ref>PMID:19854131</ref> <ref>PMID:22763445</ref> <ref>PMID:22863775</ref> <ref>PMID:25483097</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mammalian DNA polymerase-alpha-primase (Polalpha-primase) complex is essential for DNA metabolism, providing the de novo RNA-DNA primer for several DNA replication pathways(1-4) such as lagging-strand synthesis and telomere C-strand fill-in. The physical mechanism underlying how Polalpha-primase, alone or in partnership with accessory proteins, performs its complicated multistep primer synthesis function is unknown. Here we show that CST, a single-stranded DNA-binding accessory protein complex for Polalpha-primase, physically organizes the enzyme for efficient primer synthesis. Cryogenic electron microscopy structures of the CST-Polalpha-primase preinitiation complex (PIC) bound to various types of telomere overhang reveal that template-bound CST partitions the DNA and RNA catalytic centres of Polalpha-primase into two separate domains and effectively arranges them in RNA-DNA synthesis order. The architecture of the PIC provides a single solution for the multiple structural requirements for the synthesis of RNA-DNA primers by Polalpha-primase. Several insights into the template-binding specificity of CST, template requirement for assembly of the CST-Polalpha-primase PIC and activation are also revealed in this study.
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Structures of the human CST-Polalpha-primase complex bound to telomere templates.,He Q, Lin X, Chavez BL, Agrawal S, Lusk BL, Lim CJ Nature. 2022 Aug;608(7924):826-832. doi: 10.1038/s41586-022-05040-1. Epub 2022, Jul 13. PMID:35830881<ref>PMID:35830881</ref>
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==See Also==
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*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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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 8d0b" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>

Current revision

Human CST-DNA polymerase alpha/primase preinitiation complex bound to 4xTEL-foldback template

PDB ID 8d0b

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