2v1b: Difference between revisions

Revision as of 19:52, 21 February 2008

N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (ROOM TEMPERATURE (293K) 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

2V1B 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.

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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 ==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.
+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==
-V1B 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> and <scene name='pdbsite=AC2:Gol Binding Site For Chain A'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1B OCA].
+V1B 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> and <scene name='pdbsite=AC2:Gol+Binding+Site+For+Chain+A'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1B 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:[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://ispc.weizmann.ac.il//pmbin/getpm?pmid=18001137 18001137]
 [[Category: Avena sativa]]
 [[Category: Single protein]]
-[[Category: Halavaty, A.S.]]
+[[Category: Halavaty, A S.]]
 [[Category: Moffat, K.]]
 [[Category: FMN]]
@@ Line 27: / Line 27: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:46:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:52:25 2008''