Interaction of zinc ions with d(CGCAATTGCG) in a 2.9 Å resolution X-ray structure Journal Article


Authors: Soler-López, M.; Malinina, L.; Terechko, V.; Zarytova, V.; Subirana, J. A.
Article Title: Interaction of zinc ions with d(CGCAATTGCG) in a 2.9 Å resolution X-ray structure
Abstract: We have synthesized and crystallized in the presence of Zn2+ ions the peptidyl-oligonucleotide adduct CH3CO-(Arg)4-NH- (CH2)6-NH-p-d(CGCAAT-TGCG). This is the first structure obtained from a deoxyoligonucleotide crystallized in the presence of zinc ions. Zn ions are clearly visible in the 2.9 Å resolution map. On the other hand, the peptide tail is not visible in the crystal structure as determined by X-ray diffraction. The terminal bases C1 and G10 are found in extra-helical positions. Their phosphates are ligands of a Zn2+ ion, located in a special position of the unit cell. This ion plays an important role in the packing arrangement, since it binds four different DNA molecules. Two other Zn2+ ions are also important for DNA packing. They interact specifically with the N7 atoms of the terminal G2 and G10 bases, but not with the internal G8. This result supports the hypothesis that transition metals do not interact with the bases of duplex DNA in the B form.
Keywords: protein dna binding; amino terminal sequence; guanine; models, molecular; crystallography, x-ray; chemical structure; molecular interaction; nucleic acid conformation; zinc; crystallization; structure analysis; oligonucleotide; ligand binding; chemical reaction; synthesis; oligodeoxynucleotide; oligonucleotides; adenine; oligodeoxyribonucleotides; x ray analysis; x ray diffraction; transition element; thymine; x-ray diffraction; zinc ion; cytosine; priority journal; article; guanine-ion interactions; oligonucleotide structure
Journal Title: Journal of Biological Inorganic Chemistry
Volume: 7
Issue: 4-5
ISSN: 0949-8257
Publisher: Springer  
Date Published: 2002-04-01
Start Page: 533
End Page: 538
Language: English
DOI: 10.1007/s00775-001-0333-z
PUBMED: 11941511
PROVIDER: scopus
DOI/URL:
Notes: Export Date: 14 November 2014 -- Source: Scopus
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