1kaf
From Proteopedia
(New page: 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=" | + | [[Image:1kaf.gif|left|200px]]<br /><applet load="1kaf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kaf, resolution 1.6Å" /> | caption="1kaf, resolution 1.6Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Sickmier, E A.]] |
| - | [[Category: White, S | + | [[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.]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:58 2008'' |
Revision as of 11:31, 21 February 2008
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DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)
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.
About this Structure
1KAF is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
Reference
The MotA transcription factor from bacteriophage T4 contains a novel DNA-binding domain: the 'double wing' motif., Li N, Sickmier EA, Zhang R, Joachimiak A, White SW, Mol Microbiol. 2002 Mar;43(5):1079-88. PMID:11918797
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