2akg
From Proteopedia
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| - | [[Image:2akg.gif|left|200px]] | + | [[Image:2akg.gif|left|200px]] |
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| - | '''Thallium form of the G-Quadruplex from Oxytricha Nova, d(G4T4G4)2''' | + | {{Structure |
| + | |PDB= 2akg |SIZE=350|CAPTION= <scene name='initialview01'>2akg</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Thallium form of the G-Quadruplex from Oxytricha Nova, d(G4T4G4)2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AKG is a [ | + | 2AKG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AKG OCA]. |
==Reference== | ==Reference== | ||
| - | 205Tl NMR methods for the characterization of monovalent cation binding to nucleic acids., Gill ML, Strobel SA, Loria JP, J Am Chem Soc. 2005 Nov 30;127(47):16723-32. PMID:[http:// | + | 205Tl NMR methods for the characterization of monovalent cation binding to nucleic acids., Gill ML, Strobel SA, Loria JP, J Am Chem Soc. 2005 Nov 30;127(47):16723-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16305263 16305263] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Gill, M L.]] | [[Category: Gill, M L.]] | ||
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[[Category: thallium]] | [[Category: thallium]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:50:43 2008'' |
Revision as of 13:50, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Thallium form of the G-Quadruplex from Oxytricha Nova, d(G4T4G4)2
Overview
Monovalent cations play an important role in many biological functions. The guanine rich sequence, d(G4T4G4), requires monovalent cations for formation of the G-quadruplex, d(G4T4G4)2. This requirement can be satisfied by thallium (Tl+), a potassium (K+) surrogate. To verify that the structure of d(G4T4G4)2 in the presence of Tl+ is similar to the K+-form of the G-quadruplex, the solution structure of the Tl+-form of d(G4T4G4)2 was determined. The 10 lowest energy structures have an all atom RMSD of 0.76 +/- 0.16 A. Comparison of this structure to the identical G-quadruplex formed in the presence of K+ validates the isomorphous nature of Tl+ and K+. Using a 1H-205Tl spin-echo difference experiment we show that, in the Tl+-form of d(G4T4G4)2, small scalar couplings (<1 Hz) exist between 205Tl and protons in the G-quadruplex. These data comprise the first 1H-205Tl scalar couplings observed in a biological system and have the potential to provide important constraints for structure determination. These experiments can be applied to any system in which the substituted Tl+ cations are in slow exchange with the bulk ions in solution.
About this Structure
2AKG is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
205Tl NMR methods for the characterization of monovalent cation binding to nucleic acids., Gill ML, Strobel SA, Loria JP, J Am Chem Soc. 2005 Nov 30;127(47):16723-32. PMID:16305263
Page seeded by OCA on Thu Mar 20 15:50:43 2008
