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1kaf

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{{STRUCTURE_1kaf| PDB=1kaf | SCENE= }}
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'''DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)'''
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===DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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Revision as of 07:02, 2 July 2008

Image:1kaf.png

Template:STRUCTURE 1kaf

DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)

Template:ABSTRACT PUBMED 11918797

About this Structure

1KAF is a Single protein structure of sequence from Enterobacteria phage 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

Page seeded by OCA on Wed Jul 2 10:02:01 2008

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