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4HIO

Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GGTAACGGT)

Summary for 4HIO
Entry DOI10.2210/pdb4hio/pdb
Related4HID 4HIK 4HIM 4HJ5 4HJ7 4HJ8 4HJ9 4HJA
DescriptorProtection of telomeres protein 1, DNA (5'-D(*GP*GP*TP*AP*AP*CP*GP*GP*T)-3') (3 entities in total)
Functional Keywordsspecificity, plasticity, promiscuity, ob-fold, ssdna-binding, single-stranded telomeric dna, dna binding protein
Biological sourceSchizosaccharomyces pombe (Fission yeast)
More
Cellular locationNucleus: O13988
Total number of polymer chains2
Total formula weight19978.26
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 citationDickey, 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: 23201273
DOI: 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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数据于2025-07-30公开中

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