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[[Image:2v0w.jpg|left|200px]]


{{Structure
==N- and C-terminal helices of oat LOV2 (404-546) are involved in light- induced signal transduction (cryo-trapped light structure of LOV2 (404-546))==
|PDB= 2v0w |SIZE=350|CAPTION= <scene name='initialview01'>2v0w</scene>, resolution 1.70&Aring;
<StructureSection load='2v0w' size='340' side='right'caption='[[2v0w]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Fmn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Gol+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Gol+Binding+Site+For+Chain+A'>AC3</scene> and <scene name='pdbsite=AC4:Gol+Binding+Site+For+Chain+A'>AC4</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[2v0w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Avena_sativa Avena sativa]. 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=2V0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0W FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2v0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0w OCA], [https://pdbe.org/2v0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v0w RCSB], [https://www.ebi.ac.uk/pdbsum/2v0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0w ProSAT]</span></td></tr>
 
</table>
'''N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (CRYO-TRAPPED LIGHT STRUCTURE OF LOV2 (404-546))'''
== Function ==
 
[https://www.uniprot.org/uniprot/O49003_AVESA O49003_AVESA]
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/2v0w_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2v0w ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Light sensing by photoreceptors controls phototropism, chloroplast movement, stomatal opening, and leaf expansion in plants. Understanding the molecular mechanism by which these processes are regulated requires a quantitative description of photoreceptor dynamics. We focus on a light-driven signal transduction mechanism in the LOV2 domain (LOV, light, oxygen, voltage) of the blue light photoreceptor phototropin 1 from Avena sativa (oat). High-resolution crystal structures of the dark and light states of an oat LOV2 construct including residues Leu404 through Leu546 (LOV2 (404-546)) have been determined at 105 and 293 K. In all four structures, LOV2 (404-546) exhibits the typical Per-ARNT-Sim (PAS) fold, flanked by an additional conserved N-terminal turn-helix-turn motif and a C-terminal flanking region containing an amphipathic Jalpha helix. These regions dock on the LOV2 core domain and bury several hydrophobic residues of the central beta-sheet of the core domain that would otherwise be exposed to solvent. Light structures of LOV2 (404-546) reveal that formation of the covalent bond between Cys450 and the C4a atom of the flavin mononucleotide (FMN) results in local rearrangement of the hydrogen-bonding network in the FMN binding pocket. These rearrangements are associated with disruption of the Asn414-Asp515 hydrogen bond on the surface of the protein and displacement of the N- and C-terminal flanking regions of LOV2 (404-546), both of which constitute a structural signal.
Light sensing by photoreceptors controls phototropism, chloroplast movement, stomatal opening, and leaf expansion in plants. Understanding the molecular mechanism by which these processes are regulated requires a quantitative description of photoreceptor dynamics. We focus on a light-driven signal transduction mechanism in the LOV2 domain (LOV, light, oxygen, voltage) of the blue light photoreceptor phototropin 1 from Avena sativa (oat). High-resolution crystal structures of the dark and light states of an oat LOV2 construct including residues Leu404 through Leu546 (LOV2 (404-546)) have been determined at 105 and 293 K. In all four structures, LOV2 (404-546) exhibits the typical Per-ARNT-Sim (PAS) fold, flanked by an additional conserved N-terminal turn-helix-turn motif and a C-terminal flanking region containing an amphipathic Jalpha helix. These regions dock on the LOV2 core domain and bury several hydrophobic residues of the central beta-sheet of the core domain that would otherwise be exposed to solvent. Light structures of LOV2 (404-546) reveal that formation of the covalent bond between Cys450 and the C4a atom of the flavin mononucleotide (FMN) results in local rearrangement of the hydrogen-bonding network in the FMN binding pocket. These rearrangements are associated with disruption of the Asn414-Asp515 hydrogen bond on the surface of the protein and displacement of the N- and C-terminal flanking regions of LOV2 (404-546), both of which constitute a structural signal.


==About this Structure==
N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa.,Halavaty AS, Moffat K Biochemistry. 2007 Dec 11;46(49):14001-9. Epub 2007 Nov 15. PMID:18001137<ref>PMID:18001137</ref>
2V0W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Avena_sativa Avena sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0W OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa., Halavaty AS, Moffat K, Biochemistry. 2007 Dec 11;46(49):14001-9. Epub 2007 Nov 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18001137 18001137]
</div>
<div class="pdbe-citations 2v0w" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Avena sativa]]
[[Category: Avena sativa]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Halavaty, A S.]]
[[Category: Phototropin]]
[[Category: Moffat, K.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: FMN]]
[[Category: Halavaty AS]]
[[Category: GOL]]
[[Category: Moffat K]]
[[Category: atp-binding]]
[[Category: avena sativa]]
[[Category: kinase]]
[[Category: light-induced signal transduction]]
[[Category: lov2]]
[[Category: nucleotide-binding]]
[[Category: phototropin1]]
[[Category: serine/threonine-protein kinase]]
[[Category: transferase]]
 
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