3kf8

<StructureSection load='3kf8' size='340' side='right' caption='[[3kf8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[3kf8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cantt Cantt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KF8 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3key|3key]], [[3kf6|3kf6]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTRG_01841 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294747 CANTT]), CTRG_00988 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294747 CANTT])</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=3kf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kf8 OCA], [http://pdbe.org/3kf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kf8 RCSB], [http://www.ebi.ac.uk/pdbsum/3kf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kf8 ProSAT]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/3kf8_consurf.spt"</scriptWhenChecked>

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== 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<ref>PMID:20008938</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3kf8" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Cantt]]

[[Category: Confer, L A]]

[[Category: Lei, M]]

[[Category: Lue, N F]]

[[Category: Sun, J]]

[[Category: Sun, S H]]

[[Category: Wan, K]]

[[Category: Yang, Y T]]

[[Category: Yu, E Y]]

[[Category: Structural protein]]