View source for 1kaf


==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/Bpt4 Bpt4]. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bja|1bja]], [[1i1s|1i1s]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MotA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kaf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bpt4]]
[[Category: Large Structures]]
[[Category: Joachimiak, A]]
[[Category: Li, N]]
[[Category: Sickmier, E A]]
[[Category: White, S W]]
[[Category: Zhang, R]]
[[Category: Escherichia coli]]
[[Category: Eubacterial promoters]]
[[Category: Protein-dna interaction]]
[[Category: Structural genomic]]
[[Category: Transcription]]
[[Category: X-ray crystallography]]