1VTD
UNUSUAL HELICAL PACKING IN CRYSTALS OF DNA BEARING A MUTATION HOT SPOT
Summary for 1VTD
Entry DOI | 10.2210/pdb1vtd/pdb |
Descriptor | DNA (5'-D(*AP*CP*CP*GP*GP*CP*GP*CP*CP*AP*CP*A)-3'), DNA (5'-D(*TP*GP*TP*GP*GP*CP*GP*CP*CP*GP*GP*T)-3') (2 entities in total) |
Functional Keywords | b-dna, double helix, dna |
Biological source | synthetic construct More |
Total number of polymer chains | 2 |
Total formula weight | 7327.77 |
Authors | Timsit, Y.,Westhof, E.,Fuchs, R.P.P.,Moras, D. (deposition date: 1996-12-12, release date: 2011-07-13, Last modification date: 2023-12-27) |
Primary citation | Timsit, Y.,Westhof, E.,Fuchs, R.P.,Moras, D. Unusual helical packing in crystals of DNA bearing a mutation hot spot. Nature, 341:459-462, 1989 Cited by PubMed Abstract: The target sequence of the restriction enzyme NarI (GGCGCC) is a hot spot for the -2 frameshift mutagenesis (GGCGCC----GGCC) induced by the chemical carcinogens such as N-2-acetyl-aminofluorene. Of the guanine residues, all of which show equal reactivity towards the carcinogen, only binding to the 3'-most proximal guanine within the NarI site is able to trigger the frameshift event. We selected the non-palindromic dodecamer d(ACCGGCGCCACA), whose sequence corresponds to the most mutagenic NarI site in pBR322 DNA; for X-ray structure analysis. Its molecular structure determined at 2.8 A resolution reveals significant deviations from the structure of canonical B-form DNA, with partial opening of three G-C base pairs, high propeller twist values and sequence-dependent three-centred hydrogen bonds. This crystal structure shows a novel kind of packing in which helices are locked together by groove-backbone interactions. The partial opening of G-C base pairs is induced by interactions of phosphate anionic oxygen atoms with the amino group of cytosine bases. This provides a model for close approach of DNA molecules during biological processes, such as recombination. PubMed: 2797169DOI: 10.1038/341459a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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