1gau
From Proteopedia
(New page: 200px<br /><applet load="1gau" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gau" /> '''SOLUTION STRUCTURE OF THE SPECIFIC DNA COMPL...) |
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| - | [[Image:1gau.gif|left|200px]]<br /><applet load="1gau" size=" | + | [[Image:1gau.gif|left|200px]]<br /><applet load="1gau" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''SOLUTION STRUCTURE OF THE SPECIFIC DNA COMPLEX OF THE ZINC CONTAINING DNA BINDING DOMAIN OF THE ERYTHROID TRANSCRIPTION FACTOR GATA-1 BY MULTIDIMENSIONAL NMR'''<br /> | '''SOLUTION STRUCTURE OF THE SPECIFIC DNA COMPLEX OF THE ZINC CONTAINING DNA BINDING DOMAIN OF THE ERYTHROID TRANSCRIPTION FACTOR GATA-1 BY MULTIDIMENSIONAL NMR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The high-resolution three-dimensional structure of a synthetic 57-residue | + | The high-resolution three-dimensional structure of a synthetic 57-residue peptide comprising the double zinc finger of the human enhancer binding protein MBP-1 has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1280 experimental restraints. A total of 30 simulated annealing structures were calculated. The backbone atomic root-mean-square distributions about the mean coordinate positions are 0.32 and 0.33 A for the N- and C-terminal fingers, respectively, and the corresponding values for all atoms, excluding disordered surface side chains, are 0.36 and 0.40 A. Each finger comprises an irregular antiparallel sheet and a helix, with the zinc tetrahedrally coordinated to two cysteines and two histidines. The overall structure is nonglobular in nature, and the angle between the long axes of the helices is 47 +/- 5 degrees. The long axis of the antiparallel sheet in the N-terminal finger is approximately parallel to that of the helix in the C-terminal finger. Comparison of this structure with the X-ray structure of the Zif-268 triple finger complexed with DNA indicates that the relative orientation of the individual zinc fingers is clearly distinct in the two cases. This difference can be attributed to the presence of a long Lys side chain in the C-terminal finger of MBP-1 at position 40, instead of a short Ala or Ser side chain at the equivalent position in Zif-268. This finding suggests that different contacts may be involved in the binding of the zinc fingers of MBP-1 and Zif-268 to DNA, consistent with the findings from methylation interference experiments that the two fingers of MBP-1 contact 10 base pairs, while the three fingers of Zif-268 contact only 9 base pairs. |
==About this Structure== | ==About this Structure== | ||
| - | 1GAU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http:// | + | 1GAU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GAU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Clore, G | + | [[Category: Clore, G M.]] |
| - | [[Category: Gronenborn, A | + | [[Category: Gronenborn, A M.]] |
| - | [[Category: Omichinski, J | + | [[Category: Omichinski, J G.]] |
[[Category: transcription/dna]] | [[Category: transcription/dna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:04 2008'' |
Revision as of 10:48, 21 February 2008
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SOLUTION STRUCTURE OF THE SPECIFIC DNA COMPLEX OF THE ZINC CONTAINING DNA BINDING DOMAIN OF THE ERYTHROID TRANSCRIPTION FACTOR GATA-1 BY MULTIDIMENSIONAL NMR
Overview
The high-resolution three-dimensional structure of a synthetic 57-residue peptide comprising the double zinc finger of the human enhancer binding protein MBP-1 has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1280 experimental restraints. A total of 30 simulated annealing structures were calculated. The backbone atomic root-mean-square distributions about the mean coordinate positions are 0.32 and 0.33 A for the N- and C-terminal fingers, respectively, and the corresponding values for all atoms, excluding disordered surface side chains, are 0.36 and 0.40 A. Each finger comprises an irregular antiparallel sheet and a helix, with the zinc tetrahedrally coordinated to two cysteines and two histidines. The overall structure is nonglobular in nature, and the angle between the long axes of the helices is 47 +/- 5 degrees. The long axis of the antiparallel sheet in the N-terminal finger is approximately parallel to that of the helix in the C-terminal finger. Comparison of this structure with the X-ray structure of the Zif-268 triple finger complexed with DNA indicates that the relative orientation of the individual zinc fingers is clearly distinct in the two cases. This difference can be attributed to the presence of a long Lys side chain in the C-terminal finger of MBP-1 at position 40, instead of a short Ala or Ser side chain at the equivalent position in Zif-268. This finding suggests that different contacts may be involved in the binding of the zinc fingers of MBP-1 and Zif-268 to DNA, consistent with the findings from methylation interference experiments that the two fingers of MBP-1 contact 10 base pairs, while the three fingers of Zif-268 contact only 9 base pairs.
About this Structure
1GAU is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.
Reference
High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1., Omichinski JG, Clore GM, Robien M, Sakaguchi K, Appella E, Gronenborn AM, Biochemistry. 1992 Apr 28;31(16):3907-17. PMID:1567844
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