|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Crystal structure of S. cerevisiae Stn1 C-terminal== | | ==Crystal structure of S. cerevisiae Stn1 C-terminal== |
| - | <StructureSection load='3key' size='340' side='right' caption='[[3key]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3key' size='340' side='right'caption='[[3key]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3key]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KEY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3key]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KEY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kf6|3kf6]], [[3kf8|3kf8]]</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]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STN1, YDR082W, D4456, YD8554.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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=3key FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3key OCA], [https://pdbe.org/3key PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3key RCSB], [https://www.ebi.ac.uk/pdbsum/3key PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3key ProSAT]</span></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=3key FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3key OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3key RCSB], [http://www.ebi.ac.uk/pdbsum/3key PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/STN1_YEAST STN1_YEAST]] Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13.<ref>PMID:9042864</ref> <ref>PMID:11230140</ref> | + | [https://www.uniprot.org/uniprot/STN1_YEAST STN1_YEAST] Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13.<ref>PMID:9042864</ref> <ref>PMID:11230140</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 17: |
Line 17: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3key" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Confer, L A]] | + | [[Category: Confer LA]] |
| - | [[Category: Lei, M]] | + | [[Category: Lei M]] |
| - | [[Category: Lue, N F]] | + | [[Category: Lue NF]] |
| - | [[Category: Sun, J]] | + | [[Category: Sun J]] |
| - | [[Category: Sun, S H]] | + | [[Category: Sun SH]] |
| - | [[Category: Wan, K]] | + | [[Category: Wan K]] |
| - | [[Category: Yang, Y T]] | + | [[Category: Yang YT]] |
| - | [[Category: Yu, E Y]] | + | [[Category: Yu EY]] |
| - | [[Category: Butterfly wing-shaped]]
| + | |
| - | [[Category: Chromosomal protein]]
| + | |
| - | [[Category: Helix]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Telomere]]
| + | |
| Structural highlights
Function
STN1_YEAST Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13.[1] [2]
Publication Abstract from PubMed
In budding yeast, Cdc13, Stn1, and Ten1 form a heterotrimeric complex (CST) that is essential for telomere protection and maintenance. Previous bioinformatics analysis revealed a putative oligonucleotide/oligosaccharide-binding (OB) fold at the N terminus of Stn1 (Stn1N) that shows limited sequence similarity to the OB fold of Rpa2, a subunit of the eukaryotic ssDNA-binding protein complex replication protein A (RPA). Here we present functional and structural analyses of Stn1 and Ten1 from multiple budding and fission yeast. The crystal structure of the Candida tropicalis Stn1N complexed with Ten1 demonstrates an Rpa2N-Rpa3-like complex. In both structures, the OB folds of the two components pack against each other through interactions between two C-terminal helices. The structure of the C-terminal domain of Saccharomyces cerevisiae Stn1 (Stn1C) was found to comprise two related winged helix-turn-helix (WH) motifs, one of which is most similar to the WH motif at the C terminus of Rpa2, again supporting the notion that Stn1 resembles Rpa2. The crystal structure of the fission yeast Schizosaccharomyces pombe Stn1N-Ten1 complex exhibits a virtually identical architecture as the C. tropicalis Stn1N-Ten1. Functional analyses of the Candida albicans Stn1 and Ten1 proteins revealed critical roles for these proteins in suppressing aberrant telomerase and recombination activities at telomeres. Mutations that disrupt the Stn1-Ten1 interaction induce telomere uncapping and abolish the telomere localization of Ten1. Collectively, our structural and functional studies illustrate that, instead of being confined to budding yeast telomeres, the CST complex may represent an evolutionarily conserved RPA-like telomeric complex at the 3' overhangs that works in parallel with or instead of the well-characterized POT1-TPP1/TEBPalpha-beta complex.
Stn1-Ten1 is an Rpa2-Rpa3-like complex at telomeres.,Sun J, Yu EY, Yang Y, Confer LA, Sun SH, Wan K, Lue NF, Lei M Genes Dev. 2009 Dec 15;23(24):2900-14. PMID:20008938[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grandin N, Reed SI, Charbonneau M. Stn1, a new Saccharomyces cerevisiae protein, is implicated in telomere size regulation in association with Cdc13. Genes Dev. 1997 Feb 15;11(4):512-27. PMID:9042864
- ↑ Grandin N, Damon C, Charbonneau M. Ten1 functions in telomere end protection and length regulation in association with Stn1 and Cdc13. EMBO J. 2001 Mar 1;20(5):1173-83. PMID:11230140 doi:10.1093/emboj/20.5.1173
- ↑ Sun J, Yu EY, Yang Y, Confer LA, Sun SH, Wan K, Lue NF, Lei M. Stn1-Ten1 is an Rpa2-Rpa3-like complex at telomeres. Genes Dev. 2009 Dec 15;23(24):2900-14. PMID:20008938 doi:23/24/2900
|
