Sandbox122: Difference between revisions
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==Structure of LOV2== | ==Structure of LOV2== | ||
The structure of a flaving domain, LOV2, from the chimeric phototropin photoreceptor PHY3, has been determined thanks to X-Ray diffraction. This domain is composed by four chains which are identical A, B, C and D. It's a L-polypeptide which weight 50552,99 Da. Each chains has 104 aminoacids and possess four | The structure of a flaving domain, LOV2, from the chimeric phototropin photoreceptor PHY3, has been determined thanks to X-Ray diffraction. This domain is composed by four chains which are identical A, B, C and D. It's a L-polypeptide which weight 50552,99 Da. Each chains has 104 aminoacids and possess four <scene name='Sandbox122/Helix_of_the_lov2_domain/1'>helix</scene>(28 residues which represents 26%) and six B sheets (37 residues which represent 35%). | ||
==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 R983 and R967(alpha C helix) create ionic bond with phosphate group of FMN. Q970, N965, N998, N1008(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 R983 and R967(alpha C helix) create ionic bond with phosphate group of FMN. Q970, N965, N998, N1008(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. | ||
