1kaf
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(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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Revision as of 16:52, 20 November 2007
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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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