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1kaf
From Proteopedia
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| - | [[ | + | ==DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)== |
| + | <StructureSection load='1kaf' size='340' side='right' caption='[[1kaf]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1kaf]] is a 6 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KAF FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bja|1bja]], [[1i1s|1i1s]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MotA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1kaf RCSB], [http://www.ebi.ac.uk/pdbsum/1kaf PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Bpt4]] | |
| - | == | + | |
| - | < | + | |
| - | [[Category: | + | |
[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
[[Category: Li, N.]] | [[Category: Li, N.]] | ||
Revision as of 05:27, 8 June 2014
DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)
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