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| [[Image:1d48.gif|left|200px]]<br /><applet load="1d48" size="450" color="white" frame="true" align="right" spinBox="true"
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| caption="1d48, resolution 1.000Å" />
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| '''STRUCTURE OF THE PURE-SPERMINE FORM OF Z-DNA (MAGNESIUM FREE) AT 1 ANGSTROM RESOLUTION'''<br />
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| ==Overview== | | ==STRUCTURE OF THE PURE-SPERMINE FORM OF Z-DNA (MAGNESIUM FREE) AT 1 ANGSTROM RESOLUTION== |
| We describe the three-dimensional X-ray structure of a complex of spermine, bound to a Z-DNA duplex, [d(CGCGCG)]2, in the absence of any inorganic, polyvalent cations. We have crystallized the DNA hexamer d(CGCGCG) in the, exclusion of magnesium and other polyvalent ions and solved its structure, at 1.0-A resolution. In the crystal of this pure-spermine form of Z-DNA, the relative orientation, position, and interactions of the DNA differ, from the arrangement uniformly observed in over a dozen previously, reported Z-DNA hexamers. Moreover, the conformation of the Z-DNA hexamer, in this structure varies somewhat from those found in earlier structures., The DNA is compressed along the helical axis, the base pairs are shifted, into the major groove, and the minor groove is more narrow. The packing of, spermine-DNA complexes in crystals suggests that the molecular basis for, the tendency of spermine to stabilize compact DNA structures derives from, the capacity of spermine to interact simultaneously with several duplexes., This capacity is maximized by both the polymorphic nature and the length, of the spermine cation. The length and flexibility of spermine and the, dispersion of charge-charge, hydrogen-bonding, and hydrophobic bonding, potential throughout the molecule maximize the ability of spermine to, interact simultaneously with different DNA molecules.
| | <StructureSection load='1d48' size='340' side='right'caption='[[1d48]], [[Resolution|resolution]] 1.00Å' scene=''> |
| | | == Structural highlights == |
| ==About this Structure== | | <table><tr><td colspan='2'>[[1d48]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D48 FirstGlance]. <br> |
| 1D48 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with SPM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D48 OCA].
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1Å</td></tr> |
| | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SPM:SPERMINE'>SPM</scene></td></tr> |
| ==Reference==
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d48 OCA], [https://pdbe.org/1d48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d48 RCSB], [https://www.ebi.ac.uk/pdbsum/1d48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d48 ProSAT]</span></td></tr> |
| Structure of the pure-spermine form of Z-DNA (magnesium free) at 1-A resolution., Egli M, Williams LD, Gao Q, Rich A, Biochemistry. 1991 Dec 3;30(48):11388-402. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1742278 1742278]
| | </table> |
| [[Category: Protein complex]] | | __TOC__ |
| [[Category: Egli, M.]] | | </StructureSection> |
| [[Category: Gao, Q.]] | | [[Category: Large Structures]] |
| [[Category: Rich, A.]] | | [[Category: Egli M]] |
| [[Category: Williams, L.D.]] | | [[Category: Gao Q]] |
| [[Category: SPM]]
| | [[Category: Rich A]] |
| [[Category: double helix]]
| | [[Category: Williams LD]] |
| [[Category: z-dna]]
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| ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:28:05 2007''
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