1ir5
From Proteopedia
(New page: 200px<br /><applet load="1ir5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ir5" /> '''Solution Structure of the 17mer TF1 Binding ...) |
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| - | [[Image:1ir5.gif|left|200px]]<br /><applet load="1ir5" size=" | + | [[Image:1ir5.gif|left|200px]]<br /><applet load="1ir5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ir5" /> | caption="1ir5" /> | ||
'''Solution Structure of the 17mer TF1 Binding Site'''<br /> | '''Solution Structure of the 17mer TF1 Binding Site'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Transcription factor 1 (TF1), encoded by the Bacillus subtilis | + | Transcription factor 1 (TF1), encoded by the Bacillus subtilis bacteriophage SPO1, is a DNA-binding protein of the HU family. In preparation for a determination of the structure of the DNA-TF1 complex, we have studied the conformation of one core 17-mer duplex d(5'-CACTACTCTTTGTAGTG-3')-d(5'-CACTACAAAGAGTAGTG-3'). NOESY, DQF-COSY and TOCSY spectroscopy provide resonance assignments of non-exchangeable and exchangeable protons, internucleotide and interstrand proton-proton distances, and dihedral angle constraints. Restrained molecular dynamics calculations yield a family of NMR solution structures for which the RMSD is 0.7 A (all atoms). The helical twist is 34.9 degrees for the central 15 bp. Bends toward the major groove are located between the second and fourth base pairs from each end. The G12 x C23 base pair, which is bounded on each side by consecutive A x T pairs, causes a local disturbance to the DNA helix that makes the conformations of the two end segments unsymmetrical. The pyrimidine rings at T9, T10 and T11 experience more extensive rotational movement than the rest of the structure. |
==About this Structure== | ==About this Structure== | ||
| - | 1IR5 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:// | + | 1IR5 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=1IR5 OCA]. |
==Reference== | ==Reference== | ||
1H NMR studies of a 17-mer DNA duplex., Liu W, Vu HM, Kearns DR, Biochim Biophys Acta. 2002 Feb 20;1574(1):93-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11955617 11955617] | 1H NMR studies of a 17-mer DNA duplex., Liu W, Vu HM, Kearns DR, Biochim Biophys Acta. 2002 Feb 20;1574(1):93-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11955617 11955617] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Kearns, D | + | [[Category: Kearns, D R.]] |
[[Category: Liu, W.]] | [[Category: Liu, W.]] | ||
| - | [[Category: Vu, H | + | [[Category: Vu, H M.]] |
[[Category: 17mer double helix dna]] | [[Category: 17mer double helix dna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:43 2008'' |
Revision as of 11:14, 21 February 2008
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Solution Structure of the 17mer TF1 Binding Site
Overview
Transcription factor 1 (TF1), encoded by the Bacillus subtilis bacteriophage SPO1, is a DNA-binding protein of the HU family. In preparation for a determination of the structure of the DNA-TF1 complex, we have studied the conformation of one core 17-mer duplex d(5'-CACTACTCTTTGTAGTG-3')-d(5'-CACTACAAAGAGTAGTG-3'). NOESY, DQF-COSY and TOCSY spectroscopy provide resonance assignments of non-exchangeable and exchangeable protons, internucleotide and interstrand proton-proton distances, and dihedral angle constraints. Restrained molecular dynamics calculations yield a family of NMR solution structures for which the RMSD is 0.7 A (all atoms). The helical twist is 34.9 degrees for the central 15 bp. Bends toward the major groove are located between the second and fourth base pairs from each end. The G12 x C23 base pair, which is bounded on each side by consecutive A x T pairs, causes a local disturbance to the DNA helix that makes the conformations of the two end segments unsymmetrical. The pyrimidine rings at T9, T10 and T11 experience more extensive rotational movement than the rest of the structure.
About this Structure
1IR5 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
1H NMR studies of a 17-mer DNA duplex., Liu W, Vu HM, Kearns DR, Biochim Biophys Acta. 2002 Feb 20;1574(1):93-9. PMID:11955617
Page seeded by OCA on Thu Feb 21 13:14:43 2008
