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[[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;" />
'''DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)'''<br />


==Overview==
==DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)==
<StructureSection load='1kaf' size='340' side='right'caption='[[1kaf]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kaf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KAF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kaf OCA], [https://pdbe.org/1kaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kaf RCSB], [https://www.ebi.ac.uk/pdbsum/1kaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kaf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MOTA_BPT4 MOTA_BPT4] Required for the transcriptional activation of middle promoters. Middle promoters are characterized by the presence of the conserved sequence [AT]3TGCTTNA (MotA box). MotA binds directly to MotA boxes.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:11918797</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11918797 11918797]
</div>
[[Category: Bacteriophage t4]]
<div class="pdbe-citations 1kaf" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Joachimiak, A.]]
<references/>
[[Category: Li, N.]]
__TOC__
[[Category: Sickmier, E A.]]
</StructureSection>
[[Category: White, S W.]]
[[Category: Escherichia virus T4]]
[[Category: Zhang, R.]]
[[Category: Large Structures]]
[[Category: escherichia coli; x-ray crystallography; protein-dna interactions; structural genomics; eubacterial promoters.]]
[[Category: Joachimiak A]]
 
[[Category: Li N]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:58 2008''
[[Category: Sickmier EA]]
[[Category: White SW]]
[[Category: Zhang R]]

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