1kaf

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[[Image:1kaf.gif|left|200px]]
[[Image:1kaf.gif|left|200px]]
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{{Structure
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|PDB= 1kaf |SIZE=350|CAPTION= <scene name='initialview01'>1kaf</scene>, resolution 1.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1kaf", creates the "Structure Box" on the page.
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|GENE= MotA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])
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{{STRUCTURE_1kaf| PDB=1kaf | SCENE= }}
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|RELATEDENTRY=[[1bja|1BJA]], [[1i1s|1I1s]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kaf OCA], [http://www.ebi.ac.uk/pdbsum/1kaf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kaf RCSB]</span>
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'''DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)'''
'''DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)'''
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[[Category: White, S W.]]
[[Category: White, S W.]]
[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
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[[Category: escherichia coli]]
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[[Category: Escherichia coli]]
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[[Category: eubacterial promoters.]]
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[[Category: Eubacterial promoters.]]
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[[Category: protein-dna interaction]]
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[[Category: Protein-dna interaction]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: x-ray crystallography]]
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[[Category: X-ray crystallography]]
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Revision as of 19:30, 2 May 2008

Template:STRUCTURE 1kaf

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 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 Fri May 2 22:30:03 2008

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