2akg
From Proteopedia
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|PDB= 2akg |SIZE=350|CAPTION= <scene name='initialview01'>2akg</scene> | |PDB= 2akg |SIZE=350|CAPTION= <scene name='initialview01'>2akg</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2akg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2akg OCA], [http://www.ebi.ac.uk/pdbsum/2akg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2akg RCSB]</span> | ||
}} | }} | ||
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[[Category: thallium]] | [[Category: thallium]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:53:55 2008'' |
Revision as of 22:53, 30 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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