Sandbox122: Difference between revisions

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==Interaction between FMN et LOV2 domain==
==Interaction between FMN et LOV2 domain==
The <scene name='Sandbox122/Fmn_ligand/1'>FMN</scene> (Flavin MonoNucleotide) is the ligand which is responsible for the light absorption. A single molecule of FMN is bound non convalently in the interior of LOV2 domain. FMN is stabilized thanks to hydrogen bonds, Van der Waals and electrostatic interactions. For example, atoms <scene name='Sandbox122/Arg_983/1'>R983</scene> and <scene name='Sandbox122/Arg_963/1'>R967</scene>(alpha C helix) create ionic bond with phosphate group of FMN. <scene name='Sandbox122/Q970/1'>Q970</scene>, <scene name='Sandbox122/N965/1'>N965</scene> , <scene name='Sandbox122/N998/1'>N988</scene>, <scene name='Sandbox122/N1008/1'>N1008</scene> (alpha A helix and beta-strand C, D and E) aminoacid make some electrostatic interaction which stabilize FMN. Some results indicate that the majority of the FMN  in the LOV2 domain exist in the protonated form. Researcher propose a reaction mechanism that involves excited-state proton transfer, on the nanosecond time scale , from the sulfhydryl group of the conserved cysteine to the N5 atom of FMN.
The <scene name='Sandbox122/Fmn_ligand/1'>FMN</scene> (Flavin MonoNucleotide) is the ligand which is responsible for the light absorption. A single molecule of FMN is bound non convalently in the interior of LOV2 domain. FMN is stabilized thanks to hydrogen bonds, Van der Waals and electrostatic interactions. For example, atoms <scene name='Sandbox122/Arg_983/1'>R983</scene> and <scene name='Sandbox122/Arg_963/1'>R967</scene>(alpha C helix) create ionic bond with phosphate group of FMN. <scene name='Sandbox122/Q970/1'>Q970</scene>, <scene name='Sandbox122/N965/1'>N965</scene> , <scene name='Sandbox122/N998/1'>N988</scene>, <scene name='Sandbox122/N1008/1'>N1008</scene> (alpha A helix and beta-strand C, D and E) aminoacid make some electrostatic interaction which stabilize FMN. Some results indicate that the majority of the FMN  in the LOV2 domain exist in the protonated form. Researcher propose a reaction mechanism that involves excited-state proton transfer, on the nanosecond time scale , from the sulfhydryl group of the conserved cysteine to the N5 atom of FMN.
Blue light arrives on the only LOV2 <scene name='Sandbox122/Cystein_residue/1'>cystein residue</scene>(situate 4.2A from atom C(4a)) and induces formation of covalent cysteinyl-C(4a)adduct. (To explain that, refer to the scheme). Somes studies showed that temperature have an influence on that adduct. In fact, at low temperature, the microenvironment determine the reactivity of the S-H group of Cys966. A base-catalyzed mechanism for dark state recovery. Imidazole snatch proton from N5 atom of FMN and give it to the cysteine again (explain on the scheme).
Blue light arrives on the only LOV2 <scene name='Sandbox122/Cystein_residue/1'>cystein residue</scene>(situate 4.2A from atom C(4a)) and induces formation of covalent cysteinyl-C(4a)adduct. (To explain that, refer to the scheme). Somes studies showed that temperature have an influence on that adduct. In fact, at low temperature, the microenvironment determine the reactivity of the S-H group of <scene name='Sandbox122/Cys966/2'>Cys966</scene>. A base-catalyzed mechanism for dark state recovery. Imidazole snatch proton from N5 atom of FMN and give it to the cysteine again (explain on the scheme).
[[Image:Noname05.gif | thumb]]
[[Image:Noname05.gif | thumb]]