3nws

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==Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase regulatory protein Cdc13==
==Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase regulatory protein Cdc13==
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<StructureSection load='3nws' size='340' side='right' caption='[[3nws]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3nws' size='340' side='right'caption='[[3nws]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3nws]] is a 4 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=3NWS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NWS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3nws]] is a 4 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=3NWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NWS FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nwt|3nwt]]</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">CDC13, YDL220C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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=3nws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nws OCA], [https://pdbe.org/3nws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nws RCSB], [https://www.ebi.ac.uk/pdbsum/3nws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nws ProSAT]</span></td></tr>
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<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=3nws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nws OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nws RCSB], [http://www.ebi.ac.uk/pdbsum/3nws PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CDC13_YEAST CDC13_YEAST] Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomerase activity.<ref>PMID:11230149</ref> <ref>PMID:11390652</ref> <ref>PMID:10898792</ref>
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The essential yeast protein Cdc13 facilitates chromosome end replication by recruiting telomerase to telomeres, and together with its interacting partners Stn1 and Ten1, it protects chromosome ends from nucleolytic attack, thus contributing to genome integrity. Although Cdc13 has been studied extensively, the precise role of its N-terminal domain (Cdc13N) in telomere length regulation remains unclear. Here we present a structural, biochemical, and functional characterization of Cdc13N. The structure reveals that this domain comprises an oligonucleotide/oligosaccharide binding (OB) fold and is involved in Cdc13 dimerization. Biochemical data show that Cdc13N weakly binds long, single-stranded, telomeric DNA in a fashion that is directly dependent on domain oligomerization. When introduced into full-length Cdc13 in vivo, point mutations that prevented Cdc13N dimerization or DNA binding caused telomere shortening or lengthening, respectively. The multiple DNA binding domains and dimeric nature of Cdc13 offer unique insights into how it coordinates the recruitment and regulation of telomerase access to the telomeres.
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Cdc13 N-terminal dimerization, DNA binding, and telomere length regulation.,Mitchell MT, Smith JS, Mason M, Harper S, Speicher DW, Johnson FB, Skordalakes E Mol Cell Biol. 2010 Nov;30(22):5325-34. Epub 2010 Sep 13. PMID:20837709<ref>PMID:20837709</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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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Harper, S]]
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[[Category: Harper S]]
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[[Category: Johnson, F B]]
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[[Category: Johnson FB]]
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[[Category: Mason, M]]
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[[Category: Mason M]]
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[[Category: Mitchell, M T]]
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[[Category: Mitchell MT]]
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[[Category: Skordalakes, E]]
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[[Category: Skordalakes E]]
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[[Category: Smith, J S]]
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[[Category: Smith JS]]
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[[Category: Speicher, D W]]
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[[Category: Speicher DW]]
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[[Category: Cell cycle]]
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[[Category: Ob fold]]
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[[Category: Oligonucleotide/oligosaccharide binding fold - ob fold]]
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[[Category: Single stranded telomeric dna binding]]
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Current revision

Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase regulatory protein Cdc13

PDB ID 3nws

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