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2akg

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(New page: 200px<br /><applet load="2akg" size="350" color="white" frame="true" align="right" spinBox="true" caption="2akg" /> '''Thallium form of the G-Quadruplex from Oxytr...)
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[[Image:2akg.gif|left|200px]]<br /><applet load="2akg" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2akg" />
 
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'''Thallium form of the G-Quadruplex from Oxytricha Nova, d(G4T4G4)2'''<br />
 
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==Overview==
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==Thallium form of the G-Quadruplex from Oxytricha Nova, d(G4T4G4)2==
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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 (&lt;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.
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<StructureSection load='2akg' size='340' side='right'caption='[[2akg]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2akg]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AKG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2akg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2akg OCA], [https://pdbe.org/2akg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2akg RCSB], [https://www.ebi.ac.uk/pdbsum/2akg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2akg ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 (&lt;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.
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==About this Structure==
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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<ref>PMID:16305263</ref>
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2AKG is a [http://en.wikipedia.org/wiki/Protein_complex 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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16305263 16305263]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 2akg" style="background-color:#fffaf0;"></div>
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[[Category: Gill, M.L.]]
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== References ==
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[[Category: Loria, J.P.]]
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<references/>
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[[Category: Strobel, S.A.]]
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__TOC__
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[[Category: deoxyribonucleic acid]]
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</StructureSection>
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[[Category: g-quadruplex]]
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[[Category: Large Structures]]
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[[Category: thallium]]
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[[Category: Gill ML]]
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[[Category: Loria JP]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:03:51 2008''
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[[Category: Strobel SA]]

Current revision

Thallium form of the G-Quadruplex from Oxytricha Nova, d(G4T4G4)2

PDB ID 2akg

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