3p7n: Difference between revisions
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==Crystal structure of light activated transcription factor El222 from Erythrobacter litoralis== | |||
<StructureSection load='3p7n' size='340' side='right' caption='[[3p7n]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3p7n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Erythrobacter_litoralis Erythrobacter litoralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P7N FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ELI_04755 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39960 Erythrobacter litoralis])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3p7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p7n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p7n RCSB], [http://www.ebi.ac.uk/pdbsum/3p7n PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Light-oxygen-voltage (LOV) domains are blue light-activated signaling modules integral to a wide range of photosensory proteins. Upon illumination, LOV domains form internal protein-flavin adducts that generate conformational changes which control effector function. Here we advance our understanding of LOV regulation with structural, biophysical, and biochemical studies of EL222, a light-regulated DNA-binding protein. The dark-state crystal structure reveals interactions between the EL222 LOV and helix-turn-helix domains that we show inhibit DNA binding. Solution biophysical data indicate that illumination breaks these interactions, freeing the LOV and helix-turn-helix domains of each other. This conformational change has a key functional effect, allowing EL222 to bind DNA in a light-dependent manner. Our data reveal a conserved signaling mechanism among diverse LOV-containing proteins, where light-induced conformational changes trigger activation via a conserved interaction surface. | |||
Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein.,Nash AI, McNulty R, Shillito ME, Swartz TE, Bogomolni RA, Luecke H, Gardner KH Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9449-54. Epub 2011 May 23. PMID:21606338<ref>PMID:21606338</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Erythrobacter litoralis]] | [[Category: Erythrobacter litoralis]] | ||
[[Category: Luecke, H | [[Category: Luecke, H]] | ||
[[Category: McNulty, R | [[Category: McNulty, R]] | ||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Light-activated transcription factor]] | [[Category: Light-activated transcription factor]] | ||
[[Category: Lov domain]] | [[Category: Lov domain]] | ||
Revision as of 06:32, 19 December 2014
Crystal structure of light activated transcription factor El222 from Erythrobacter litoralis
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