2hbn
From Proteopedia
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| , resolution 1.550Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystallization of the Tl+-form of the Oxytricha nova G-quadruplex
Overview
The crystal structure of the Tl+ form of the G-quadruplex formed from the Oxytricha nova telomere sequence, d(G4T4G4), has been solved to 1.55 A. This G-quadruplex contains five Tl+ ions, three of which are interspersed between adjacent G-quartet planes and one in each of the two thymine loops. The structure displays a high degree of similarity to the K+ crystal structure [Haider et al. (2002), J. Mol. Biol., 320, 189-200], including the number and location of the monovalent cation binding sites. The highly isomorphic nature of the two structures, which contain such a large number of monovalent binding sites (relative to nucleic acid content), verifies the ability of Tl+ to mimic K+ in nucleic acids. Information from this report confirms and extends the assignment of 205Tl resonances from a previous report [Gill et al. (2005), J. Am. Chem. Soc., 127, 16 723-16 732] where 205Tl NMR was used to study monovalent cation binding to this G-quadruplex. The assignment of these resonances provides evidence for the occurrence of conformational dynamics in the thymine loop region that is in slow exchange on the 205Tl timescale.
About this Structure
2HBN is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Crystallization and characterization of the thallium form of the Oxytricha nova G-quadruplex., Gill ML, Strobel SA, Loria JP, Nucleic Acids Res. 2006;34(16):4506-14. Epub 2006 Aug 31. PMID:16945956
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