View source for 4hik


==Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GGTTACGGT)==
<StructureSection load='4hik' size='340' side='right'caption='[[4hik]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hik]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HIK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.636&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4hik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hik OCA], [https://pdbe.org/4hik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hik RCSB], [https://www.ebi.ac.uk/pdbsum/4hik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hik ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/POT1_SCHPO POT1_SCHPO] Single-stranded telomeric DNA-binding protein that is required to protect the 3'-end telomeric overhang. It binds the consensus sequence 5'-GGTTAC-3'. Regulates telomerase and telomere length.<ref>PMID:11349150</ref> <ref>PMID:12463756</ref> <ref>PMID:18535244</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pot1 is the protein responsible for binding to and protecting the 3' single-stranded DNA (ssDNA) overhang at most eukaryotic telomeres. Here, we present the crystal structure of one of the two oligonucleotide/oligosaccharide-binding folds (Pot1pC) that make up the ssDNA-binding domain in S. pombe Pot1. Comparison with the homologous human domain reveals unexpected structural divergence in the mode of ligand binding that explains the differing ligand requirements between species. Despite the presence of apparently base-specific hydrogen bonds, Pot1pC is able to bind a wide range of ssDNA sequences with thermodynamic equivalence. To address how Pot1pC binds ssDNA with little to no specificity, multiple structures of Pot1pC bound to noncognate ssDNA ligands were solved. These structures reveal that this promiscuity is implemented through new binding modes that thermodynamically compensate for base-substitutions through alternate stacking interactions and new H-bonding networks.

Nonspecific Recognition Is Achieved in Pot1pC through the Use of Multiple Binding Modes.,Dickey TH, McKercher MA, Wuttke DS Structure. 2012 Nov 28. pii: S0969-2126(12)00411-X. doi:, 10.1016/j.str.2012.10.015. PMID:23201273<ref>PMID:23201273</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hik" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe 972h-]]
[[Category: Dickey TH]]
[[Category: Wuttke DS]]