1d8g
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| , resolution 0.74Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
ULTRAHIGH RESOLUTION CRYSTAL STRUCTURE OF B-DNA DECAMER D(CCAGTACTGG)
OverviewOverview
The affinity and specificity of a ligand for its DNA site is a function of the conformational changes between the isolated and complexed states. Although the structures of a hydroxypyrrole-imidazole-pyrrole polyamide dimer with 5'-CCAGTACTGG-3' and the trp repressor recognizing the sequence 5'-GTACT-3' are known, the baseline conformation of the DNA site would contribute to our understanding of DNA recognition by these ligands. The 0.74 A resolution structure of a B-DNA double helix, 5'-CCAGTACTGG-3', has been determined by X-ray crystallography. Six of the nine phosphates, two of four bound calcium ions and networks of water molecules hydrating the oligonucleotide have alternate conformations. By contrast, nine of the ten bases have a single, unique conformation with hydrogen atoms visible in most cases. The polyamide molecules alter the geometry of the phosphodiester backbone, and the water molecules mediating contacts in the trp repressor/operator complex are conserved in the unliganded DNA. Furthermore, the multiple conformational states, ions and hydration revealed by this ultrahigh resolution structure of a B-form oligonucleotide are potentially general considerations for understanding DNA-binding affinity and specificity by ligands.
About this StructureAbout this Structure
1D8G is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Conformational flexibility of B-DNA at 0.74 A resolution: d(CCAGTACTGG)(2)., Kielkopf CL, Ding S, Kuhn P, Rees DC, J Mol Biol. 2000 Feb 25;296(3):787-801. PMID:10677281
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