4HIO
Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GGTAACGGT)
Summary for 4HIO
Entry DOI | 10.2210/pdb4hio/pdb |
Related | 4HID 4HIK 4HIM 4HJ5 4HJ7 4HJ8 4HJ9 4HJA |
Descriptor | Protection of telomeres protein 1, DNA (5'-D(*GP*GP*TP*AP*AP*CP*GP*GP*T)-3') (3 entities in total) |
Functional Keywords | specificity, plasticity, promiscuity, ob-fold, ssdna-binding, single-stranded telomeric dna, dna binding protein |
Biological source | Schizosaccharomyces pombe (Fission yeast) More |
Cellular location | Nucleus: O13988 |
Total number of polymer chains | 2 |
Total formula weight | 19978.26 |
Authors | Dickey, T.H.,McKercher, M.A.,Wuttke, D.S. (deposition date: 2012-10-11, release date: 2012-12-12, Last modification date: 2023-09-20) |
Primary citation | Dickey, T.H.,McKercher, M.A.,Wuttke, D.S. Nonspecific Recognition Is Achieved in Pot1pC through the Use of Multiple Binding Modes. Structure, 21:121-132, 2013 Cited by PubMed Abstract: 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. PubMed: 23201273DOI: 10.1016/j.str.2012.10.015 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.753 Å) |
Structure validation
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