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1d93

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(New page: 200px<br /><applet load="1d93" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d93, resolution 2.150&Aring;" /> '''STRUCTURAL VARIATIO...)
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caption="1d93, resolution 2.150&Aring;" />
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'''STRUCTURAL VARIATION IN D(CTCTAGAG). IMPLICATIONS FOR PROTEIN-DNA INTERACTIONS'''<br />
'''STRUCTURAL VARIATION IN D(CTCTAGAG). IMPLICATIONS FOR PROTEIN-DNA INTERACTIONS'''<br />
==Overview==
==Overview==
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Single-crystal X-ray diffraction techniques have been used to characterize, the structure of the self-complementary DNA oligomer d(CTCTAGAG). The, structure was refined to an R factor of 14.7% using data to 2.15-A, resolution. The tetragonal unit cell, space group P4(3)2(1)2, has, dimensions a = 42.53 and c = 24.33 A. The asymmetric unit consists of a, single strand or four base pairs. Two strands, related by a, crystallographic dyad axis, coil about each other to form a right-handed, duplex. This octamer duplex has a mean helix rotation of 32 degrees, 11.3, base pairs per turn, an average rise of 3.1 A, C3'-endo furanose, conformations, a shallow minor groove, and a deep major groove. Such, averaged parameters suggest classification of the octamer as a member of, the A-DNA family. However, the global parameters tend to mask variations, in conformational parameters observed at the level of the base pairs. In, particular, the central TpA (= TpA) step displays extensive interstrand, purine-purine overlap and an unusual sugar-phosphate backbone, conformation. These structural features may be directly related to certain, sequence-specific protein-DNA interactions involving nucleases and, repressors.
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Single-crystal X-ray diffraction techniques have been used to characterize the structure of the self-complementary DNA oligomer d(CTCTAGAG). The structure was refined to an R factor of 14.7% using data to 2.15-A resolution. The tetragonal unit cell, space group P4(3)2(1)2, has dimensions a = 42.53 and c = 24.33 A. The asymmetric unit consists of a single strand or four base pairs. Two strands, related by a crystallographic dyad axis, coil about each other to form a right-handed duplex. This octamer duplex has a mean helix rotation of 32 degrees, 11.3 base pairs per turn, an average rise of 3.1 A, C3'-endo furanose conformations, a shallow minor groove, and a deep major groove. Such averaged parameters suggest classification of the octamer as a member of the A-DNA family. However, the global parameters tend to mask variations in conformational parameters observed at the level of the base pairs. In particular, the central TpA (= TpA) step displays extensive interstrand purine-purine overlap and an unusual sugar-phosphate backbone conformation. These structural features may be directly related to certain sequence-specific protein-DNA interactions involving nucleases and repressors.
==About this Structure==
==About this Structure==
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1D93 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D93 OCA].
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1D93 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=1D93 OCA].
==Reference==
==Reference==
Structural variation in d(CTCTAGAG). Implications for protein-DNA interactions., Hunter WN, D'Estaintot BL, Kennard O, Biochemistry. 1989 Mar 21;28(6):2444-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2730875 2730875]
Structural variation in d(CTCTAGAG). Implications for protein-DNA interactions., Hunter WN, D'Estaintot BL, Kennard O, Biochemistry. 1989 Mar 21;28(6):2444-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2730875 2730875]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Estaintot, B.Langlois.D.]]
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[[Category: Estaintot, B Langlois D.]]
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[[Category: Hunter, W.N.]]
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[[Category: Hunter, W N.]]
[[Category: Kennard, O.]]
[[Category: Kennard, O.]]
[[Category: a-dna]]
[[Category: a-dna]]
[[Category: double helix]]
[[Category: double helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:47:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:14 2008''

Revision as of 10:14, 21 February 2008


1d93, resolution 2.150Å

Drag the structure with the mouse to rotate

STRUCTURAL VARIATION IN D(CTCTAGAG). IMPLICATIONS FOR PROTEIN-DNA INTERACTIONS

Overview

Single-crystal X-ray diffraction techniques have been used to characterize the structure of the self-complementary DNA oligomer d(CTCTAGAG). The structure was refined to an R factor of 14.7% using data to 2.15-A resolution. The tetragonal unit cell, space group P4(3)2(1)2, has dimensions a = 42.53 and c = 24.33 A. The asymmetric unit consists of a single strand or four base pairs. Two strands, related by a crystallographic dyad axis, coil about each other to form a right-handed duplex. This octamer duplex has a mean helix rotation of 32 degrees, 11.3 base pairs per turn, an average rise of 3.1 A, C3'-endo furanose conformations, a shallow minor groove, and a deep major groove. Such averaged parameters suggest classification of the octamer as a member of the A-DNA family. However, the global parameters tend to mask variations in conformational parameters observed at the level of the base pairs. In particular, the central TpA (= TpA) step displays extensive interstrand purine-purine overlap and an unusual sugar-phosphate backbone conformation. These structural features may be directly related to certain sequence-specific protein-DNA interactions involving nucleases and repressors.

About this Structure

1D93 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Structural variation in d(CTCTAGAG). Implications for protein-DNA interactions., Hunter WN, D'Estaintot BL, Kennard O, Biochemistry. 1989 Mar 21;28(6):2444-51. PMID:2730875

Page seeded by OCA on Thu Feb 21 12:14:14 2008

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