3k10

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<StructureSection load='3k10' size='340' side='right'caption='[[3k10]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3k10' size='340' side='right'caption='[[3k10]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3k10]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K10 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3k10]] 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=3K10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K10 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3k0x|3k0x]]</div></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">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D4456, STN1, YD8554.15, YDR082W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3k10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k10 OCA], [https://pdbe.org/3k10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k10 RCSB], [https://www.ebi.ac.uk/pdbsum/3k10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k10 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=3k10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k10 OCA], [https://pdbe.org/3k10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k10 RCSB], [https://www.ebi.ac.uk/pdbsum/3k10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k10 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Telomeres must be capped to preserve chromosomal stability. The conserved Stn1 and Ten1 proteins are required for proper capping of the telomere, although the mechanistic details of how they contribute to telomere maintenance are unclear. Here, we report the crystal structures of the C-terminal domain of the Saccharomyces cerevisiae Stn1 and the Schizosaccharomyces pombe Ten1 proteins. These structures reveal striking similarities to corresponding subunits in the replication protein A complex, further supporting an evolutionary link between telomere maintenance proteins and DNA repair complexes. Our structural and in vivo data of Stn1 identify a new domain that has evolved to support a telomere-specific role in chromosome maintenance. These findings endorse a model of an evolutionarily conserved mechanism of DNA maintenance that has developed as a result of increased chromosomal structural complexity.
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Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain.,Gelinas AD, Paschini M, Reyes FE, Heroux A, Batey RT, Lundblad V, Wuttke DS Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19298-303. Epub 2009 Nov 2. PMID:19884503<ref>PMID:19884503</ref>
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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 3k10" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Batey, R T]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Gelinas, A D]]
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[[Category: Batey RT]]
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[[Category: Reyes, F E]]
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[[Category: Gelinas AD]]
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[[Category: Wuttke, D S]]
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[[Category: Reyes FE]]
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[[Category: Chromosomal protein]]
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[[Category: Wuttke DS]]
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[[Category: Phosphoprotein]]
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[[Category: Protein binding]]
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[[Category: Telomere]]
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[[Category: Telomere capping]]
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[[Category: Winged helix turn helix]]
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Revision as of 08:44, 7 February 2024

Crystal structure of telomere capping protein Stn1 from Saccharomyces cerevisiae

PDB ID 3k10

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