5dfn: Difference between revisions

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OCA

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 ==Structure of Tetrahymena Telomerase P45 C-terminal domain==
-<StructureSection load='5dfn' size='340' side='right' caption='[[5dfn]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
+<StructureSection load='5dfn' size='340' side='right'caption='[[5dfn]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5dfn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DFN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5dfn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DFN FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dfm|5dfm]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.382&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfn OCA], [http://pdbe.org/5dfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dfn RCSB], [http://www.ebi.ac.uk/pdbsum/5dfn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dfn 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=5dfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfn OCA], [https://pdbe.org/5dfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dfn RCSB], [https://www.ebi.ac.uk/pdbsum/5dfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dfn ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/TAP45_TETTS TAP45_TETTS] Component of a CST-like subcomplex of the holoenzyme telomerase ribonucleoprotein complex, which stimulates telomerase complementary-strand synthesis (PubMed:26551074). Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:26551074). The CST-like subcomplex (also named 7-4-1) binds telomeric single-stranded DNA and coordinates telomere G-strand and C-strand synthesis (PubMed:26551074).<ref>PMID:26551074</ref>
-Telomerase helps maintain telomeres by processive synthesis of telomere repeat DNA at their 3'-ends, using an integral telomerase RNA (TER) and telomerase reverse transcriptase (TERT). We report the cryo-electron microscopy structure of Tetrahymena telomerase at ~9 angstrom resolution. In addition to seven known holoenzyme proteins, we identify two additional proteins that form a complex (TEB) with single-stranded telomere DNA-binding protein Teb1, paralogous to heterotrimeric replication protein A (RPA). The p75-p45-p19 subcomplex is identified as another RPA-related complex, CST (CTC1-STN1-TEN1). This study reveals the paths of TER in the TERT-TER-p65 catalytic core and single-stranded DNA exit; extensive subunit interactions of the TERT essential N-terminal domain, p50, and TEB; and other subunit identities and structures, including p19 and p45C crystal structures. Our findings provide structural and mechanistic insights into telomerase holoenzyme function.
-Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.,Jiang J, Chan H, Cash DD, Miracco EJ, Ogorzalek Loo RR, Upton HE, Cascio D, O'Brien Johnson R, Collins K, Loo JA, Zhou ZH, Feigon J Science. 2015 Oct 30;350(6260):aab4070. doi: 10.1126/science.aab4070. Epub 2015, Oct 15. PMID:26472759<ref>PMID:26472759</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5dfn" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 23: / Line 16: @@
 __TOC__
 </StructureSection>
-[[Category: Cascio, D]]
+[[Category: Large Structures]]
-[[Category: Chan, H]]
+[[Category: Tetrahymena thermophila]]
-[[Category: Feigon, J]]
+[[Category: Cascio D]]
-[[Category: Sawaya, M R]]
+[[Category: Chan H]]
-[[Category: Cst complex]]
+[[Category: Feigon J]]
-[[Category: Nuclear protein]]
+[[Category: Sawaya MR]]
-[[Category: P45]]
-[[Category: Stn1]]
-[[Category: Telomerase]]
-[[Category: Wh domain]]
-[[Category: Whth]]
-[[Category: Winged helix]]
-[[Category: Winged helix turn helix]]