2v0w: Difference between revisions

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[[Image:2v0w.jpg|left|200px]]<br /><applet load="2v0w" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2v0w.jpg|left|200px]]
caption="2v0w, resolution 1.70&Aring;" />
 
'''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))'''<br />
{{Structure
|PDB= 2v0w |SIZE=350|CAPTION= <scene name='initialview01'>2v0w</scene>, resolution 1.70&Aring;
|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>
|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY=
|GENE=
}}
 
'''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))'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2V0W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Avena_sativa Avena sativa] with <scene name='pdbligand=FMN:'>FMN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0W OCA].  
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==
==Reference==
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=18001137 18001137]
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]
[[Category: Avena sativa]]
[[Category: Avena sativa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transferase]]
[[Category: transferase]]


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Revision as of 19:42, 20 March 2008

File:2v0w.jpg


PDB ID 2v0w

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, resolution 1.70Å
Sites: , , and
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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))


OverviewOverview

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 StructureAbout this Structure

2V0W is a Single protein structure of sequence from Avena sativa. Full crystallographic information is available from OCA.

ReferenceReference

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

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