|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of light activated transcription factor El222 from Erythrobacter litoralis== | | ==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=''> | + | <StructureSection load='3p7n' size='340' side='right'caption='[[3p7n]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3p7n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Erylh Erylh]. The March 2015 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phototropin'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2015_3 10.2210/rcsb_pdb/mom_2015_3]. 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> | + | <table><tr><td colspan='2'>[[3p7n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Erythrobacter_litoralis_HTCC2594 Erythrobacter litoralis HTCC2594]. The March 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phototropin'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_3 10.2210/rcsb_pdb/mom_2015_3]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=314225 ERYLH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></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://pdbe.org/3p7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3p7n RCSB], [http://www.ebi.ac.uk/pdbsum/3p7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3p7n 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=3p7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p7n OCA], [https://pdbe.org/3p7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p7n RCSB], [https://www.ebi.ac.uk/pdbsum/3p7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p7n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LVHTH_ERYLH LVHTH_ERYLH] Has reversible, light-dependent DNA-binding activity. Upon illumination an internal FMN-protein adduct is formed which changes the protein conformation so that the previously sequestered DNA-binding domain is free to bind DNA. Binds to sequences within in its own promoter when illuminated but not when it has been incubated in the dark.<ref>PMID:21606338</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Erylh]] | + | [[Category: Erythrobacter litoralis HTCC2594]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Phototropin]] | | [[Category: Phototropin]] |
| | [[Category: RCSB PDB Molecule of the Month]] | | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Luecke, H]] | + | [[Category: Luecke H]] |
| - | [[Category: McNulty, R]] | + | [[Category: McNulty R]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Light-activated transcription factor]]
| + | |
| - | [[Category: Lov domain]]
| + | |
| Structural highlights
Function
LVHTH_ERYLH Has reversible, light-dependent DNA-binding activity. Upon illumination an internal FMN-protein adduct is formed which changes the protein conformation so that the previously sequestered DNA-binding domain is free to bind DNA. Binds to sequences within in its own promoter when illuminated but not when it has been incubated in the dark.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nash AI, McNulty R, Shillito ME, Swartz TE, Bogomolni RA, Luecke H, Gardner KH. Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein. Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9449-54. Epub 2011 May 23. PMID:21606338 doi:10.1073/pnas.1100262108
- ↑ Nash AI, McNulty R, Shillito ME, Swartz TE, Bogomolni RA, Luecke H, Gardner KH. Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein. Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9449-54. Epub 2011 May 23. PMID:21606338 doi:10.1073/pnas.1100262108
|
