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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 1.6&Aring;" /> '''DNA Binding Domain Of...)
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[[Image:1kaf.gif|left|200px]]<br /><applet load="1kaf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kaf, resolution 1.6&Aring;" />
 
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'''DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)'''<br />
 
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==Overview==
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==DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)==
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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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<StructureSection load='1kaf' size='340' side='right'caption='[[1kaf]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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==
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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>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KAF OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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[[Category: Bacteriophage t4]]
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<div class="pdbe-citations 1kaf" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Joachimiak, A.]]
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<references/>
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[[Category: Li, N.]]
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__TOC__
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[[Category: Sickmier, E.A.]]
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</StructureSection>
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[[Category: White, S.W.]]
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[[Category: Escherichia virus T4]]
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[[Category: Zhang, R.]]
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[[Category: Large Structures]]
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[[Category: escherichia coli; x-ray crystallography; protein-dna interactions; structural genomics; eubacterial promoters.]]
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[[Category: Joachimiak A]]
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[[Category: Li N]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:00:00 2007''
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[[Category: Sickmier EA]]
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[[Category: White SW]]
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[[Category: Zhang R]]

Current revision

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

PDB ID 1kaf

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