2v0u
From Proteopedia
(New page: 200px<br /><applet load="2v0u" size="350" color="white" frame="true" align="right" spinBox="true" caption="2v0u, resolution 1.40Å" /> '''N- AND C-TERMINAL HE...) |
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==Overview== | ==Overview== | ||
| - | Light sensing by photoreceptors controls phototropism, chloroplast | + | 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== | ==About this Structure== | ||
| - | 2V0U 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>, <scene name='pdbsite=AC4:Gol Binding Site For Chain A'>AC4</scene>, <scene name='pdbsite=AC5:Gol Binding Site For Chain A'>AC5</scene>, <scene name='pdbsite=AC6:Gol Binding Site For Chain A'>AC6</scene> and <scene name='pdbsite=AC7:Gol Binding Site For Chain A'>AC7</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0U OCA]. | + | 2V0U 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>, <scene name='pdbsite=AC4:Gol+Binding+Site+For+Chain+A'>AC4</scene>, <scene name='pdbsite=AC5:Gol+Binding+Site+For+Chain+A'>AC5</scene>, <scene name='pdbsite=AC6:Gol+Binding+Site+For+Chain+A'>AC6</scene> and <scene name='pdbsite=AC7:Gol+Binding+Site+For+Chain+A'>AC7</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0U OCA]. |
==Reference== | ==Reference== | ||
| - | N- and C- | + | 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] |
[[Category: Avena sativa]] | [[Category: Avena sativa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Halavaty, A | + | [[Category: Halavaty, A S.]] |
[[Category: Moffat, K.]] | [[Category: Moffat, K.]] | ||
[[Category: FMN]] | [[Category: FMN]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:52:15 2008'' |
Revision as of 16:52, 21 February 2008
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N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (CRYO DARK STRUCTURE OF LOV2 (404-546))
Overview
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
2V0U is a Single protein structure of sequence from Avena sativa with and as ligands. Known structural/functional Sites: , , , , , and . Full crystallographic information is available from OCA.
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:18001137
Page seeded by OCA on Thu Feb 21 18:52:15 2008
