1kaf: Difference between revisions
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<StructureSection load='1kaf' size='340' side='right'caption='[[1kaf]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1kaf' size='340' side='right'caption='[[1kaf]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kaf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | </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> | ||
<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> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia virus T4]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Joachimiak | [[Category: Joachimiak A]] | ||
[[Category: Li | [[Category: Li N]] | ||
[[Category: Sickmier | [[Category: Sickmier EA]] | ||
[[Category: White | [[Category: White SW]] | ||
[[Category: Zhang | [[Category: Zhang R]] | ||
Revision as of 12:42, 21 December 2022
DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)DNA Binding Domain Of The Phage T4 Transcription Factor MotA (AA105-211)
Structural highlights
FunctionMOTA_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. Publication Abstract from PubMedMotA 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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