138d: Difference between revisions
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[[Image:138d.gif|left|200px]] | [[Image:138d.gif|left|200px]] | ||
'''A-DNA DECAMER D(GCGGGCCCGC)-HEXAGONAL CRYSTAL FORM''' | {{Structure | ||
|PDB= 138d |SIZE=350|CAPTION= <scene name='initialview01'>138d</scene>, resolution 1.800Å | |||
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'''A-DNA DECAMER D(GCGGGCCCGC)-HEXAGONAL CRYSTAL FORM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
138D is a [ | 138D 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=138D OCA]. | ||
==Reference== | ==Reference== | ||
Evidence for crystal environment dominating base sequence effects on DNA conformation: crystal structures of the orthorhombic and hexagonal polymorphs of the A-DNA decamer d(GCGGGCCCGC) and comparison with their isomorphous crystal structures., Ramakrishnan B, Sundaralingam M, Biochemistry. 1993 Oct 26;32(42):11458-68. PMID:[http:// | Evidence for crystal environment dominating base sequence effects on DNA conformation: crystal structures of the orthorhombic and hexagonal polymorphs of the A-DNA decamer d(GCGGGCCCGC) and comparison with their isomorphous crystal structures., Ramakrishnan B, Sundaralingam M, Biochemistry. 1993 Oct 26;32(42):11458-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8218212 8218212] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ramakrishnan, B.]] | [[Category: Ramakrishnan, B.]] | ||
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[[Category: double helix]] | [[Category: double helix]] | ||
''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 09:49:18 2008'' | ||
Revision as of 10:49, 20 March 2008
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A-DNA DECAMER D(GCGGGCCCGC)-HEXAGONAL CRYSTAL FORM
OverviewOverview
We have determined the structure of the A-DNA decamer d(GCGGGCCCGC) in two crystal forms, orthorhombic and hexagonal, at 1.7- and 1.8-A resolution, respectively. In the orthorhombic form, the fifth guanine residue has nearly trans-trans conformations for the alpha-gamma backbone torsions, as in the isomorphous orthorhombic structure d(CCCGGCCGGG) [Ramakrishnan, B., & Sundaralingam, M. (1993) J. Mol. Biol. 231, 431-444]. However, in the hexagonal form, the eighth cytosine residue adopts the trans-trans conformations for the backbone alpha-gamma torsions, as in the isomorphous hexagonal structure d(ACCGGCCGGT) [Frederick, C. A., Quigley, G. J., Teng, M.-K., Coll, M., van der Marel, G. A., van Boom, J. H., Rich, A., & Wang, A. H.-J. (1989) Eur. J. Biochem. 181, 295-307]. Even though the average helix and base-pair parameters are nearly the same in the two polymorphous crystal forms having the same sequence, many of the base-dependent local helix parameters are quite different. However, in the isomorphous crystal forms, in spite of the differing base sequences, the local helix and base-pair parameters of the duplexes are nearly the same. This indicates that, in crystals, the local conformation of a DNA structure is affected severely by the crystal packing environment rather than by the base sequence.
About this StructureAbout this Structure
138D is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Evidence for crystal environment dominating base sequence effects on DNA conformation: crystal structures of the orthorhombic and hexagonal polymorphs of the A-DNA decamer d(GCGGGCCCGC) and comparison with their isomorphous crystal structures., Ramakrishnan B, Sundaralingam M, Biochemistry. 1993 Oct 26;32(42):11458-68. PMID:8218212
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