8soj: Difference between revisions

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-'''Unreleased structure'''
-The entry 8soj is ON HOLD
+==Cryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the absence of telomeric ssDNA==
+<StructureSection load='8soj' size='340' side='right'caption='[[8soj]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8soj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterovirus_A71 Enterovirus A71], [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SOJ FirstGlance]. <br>
+</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=8soj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8soj OCA], [https://pdbe.org/8soj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8soj RCSB], [https://www.ebi.ac.uk/pdbsum/8soj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8soj ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[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 ==
+[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> [https://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+CST-Polalpha/Primase maintains telomeres through fill-in synthesis of the C-rich telomeric DNA. We report cryo-EM structures that reveal how human CST is recruited to telomeres by the shelterin subunits POT1 and TPP1. CST-POT1/TPP1 is formed through interactions between POT1 and the Ctc1 subunit of CST. Coats plus syndrome mutations map to the POT1-Ctc1 interface, providing mechanistic insights into this disease. CST-POT1/TPP1 is compatible with the previously reported inactive recruitment complex of CST-Polalpha/Primase but not with the distinct conformation of active CST-Polalpha/Primase. We propose that shelterin both recruits and regulates CST-Polalpha/Primase. Structural and biochemical data indicate that this regulation involves phosphorylation of POT1, which promotes CST-POT1/TPP1 interaction and recruitment, whereas POT1 dephosphorylation releases CST-Polalpha/Primase for fill-in synthesis. ONE-SENTENCE SUMMARY: Cryo-EM structures reveal how telomere maintenance factors are recruited and regulated by the shelterin complex.
-Authors:
+Structural basis of CST-Polalpha/Primase recruitment and regulation by POT1 at telomeres.,Cai SW, Takai H, Walz T, de Lange T bioRxiv. 2023 May 9:2023.05.08.539880. doi: 10.1101/2023.05.08.539880. Preprint. PMID:37215005<ref>PMID:37215005</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8soj" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Enterovirus A71]]
+[[Category: Escherichia coli O157:H7]]
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Cai SW]]