1kaf: Difference between revisions

New page: left|200px<br /><applet load="1kaf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kaf, resolution 1.6Å" /> '''DNA Binding Domain Of...
 
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[[Image:1kaf.gif|left|200px]]<br /><applet load="1kaf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kaf.gif|left|200px]]<br /><applet load="1kaf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kaf, resolution 1.6&Aring;" />
caption="1kaf, resolution 1.6&Aring;" />
'''DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)'''<br />
'''DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)'''<br />


==Overview==
==Overview==
MotA is a transcription factor from bacteriophage T4 that helps adapt the, host Escherichia coli transcription apparatus to T4 middle promoters. We, have determined the crystal structure of the C-terminal DNA-binding domain, of MotA (MotCF) to 1.6 A resolution using multiwavelength, anomalous, diffraction methods. The structure reveals a novel DNA-binding alpha/beta, motif that contains an exposed beta-sheet surface that mediates, interactions with the DNA. Independent biochemical experiments have shown, that MotCF binds to one surface of a single turn of DNA through, interactions in adjacent major and minor grooves. We present a model of, the interaction in which beta-ribbons at opposite corners of the, six-stranded beta-sheet penetrate the DNA grooves, and call the motif a, 'double wing' to emphasize similarities to the 'winged-helix' motif. The, model is consistent with data on how MotA functions at middle promoters, and provides an explanation for why MotA can form non-specific multimers, on DNA.
MotA is a transcription factor from bacteriophage T4 that helps adapt the host Escherichia coli transcription apparatus to T4 middle promoters. We have determined the crystal structure of the C-terminal DNA-binding domain of MotA (MotCF) to 1.6 A resolution using multiwavelength, anomalous diffraction methods. The structure reveals a novel DNA-binding alpha/beta motif that contains an exposed beta-sheet surface that mediates interactions with the DNA. Independent biochemical experiments have shown that MotCF binds to one surface of a single turn of DNA through interactions in adjacent major and minor grooves. We present a model of the interaction in which beta-ribbons at opposite corners of the six-stranded beta-sheet penetrate the DNA grooves, and call the motif a 'double wing' to emphasize similarities to the 'winged-helix' motif. The model is consistent with data on how MotA functions at middle promoters, and provides an explanation for why MotA can form non-specific multimers on DNA.


==About this Structure==
==About this Structure==
1KAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KAF OCA].  
1KAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAF OCA].  


==Reference==
==Reference==
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[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
[[Category: Li, N.]]
[[Category: Li, N.]]
[[Category: Sickmier, E.A.]]
[[Category: Sickmier, E A.]]
[[Category: White, S.W.]]
[[Category: White, S W.]]
[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
[[Category: escherichia coli; x-ray crystallography; protein-dna interactions; structural genomics; eubacterial promoters.]]
[[Category: escherichia coli; x-ray crystallography; protein-dna interactions; structural genomics; eubacterial promoters.]]


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