User:Mitchell Long/Sandbox 1: Difference between revisions
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The catalytic α subunit houses the FMN cofactor and is connected to the β subunit via a hairpin structure called the "<scene name='User:Mitchell_Long/Sandbox_1/Protease_labile_region/3'>TextToBeDisplayed</scene>." The organic substrate for bacterial luciferase in vivo is myristic aldehyde, although many aliphatic aldehydes of various lengths can induce bioluminescence in vitro. | The catalytic α subunit houses the FMN cofactor and is connected to the β subunit via a hairpin structure called the "<scene name='User:Mitchell_Long/Sandbox_1/Protease_labile_region/3'>TextToBeDisplayed</scene>." The organic substrate for bacterial luciferase in vivo is myristic aldehyde, although many aliphatic aldehydes of various lengths can induce bioluminescence in vitro. | ||
<scene name='User:Mitchell_Long/Sandbox_1/Luciferase_w_out_cofactor/1'>TextToBeDisplayed</scene> | <scene name='User:Mitchell_Long/Sandbox_1/Luciferase_w_out_cofactor/1'>TextToBeDisplayed</scene> | ||
<scene name='User:Mitchell_Long/Sandbox_1/Hetero_fmn_complex_translucent/1'>TextToBeDisplayed</scene> | |||
<scene name='User:Mitchell_Long/Sandbox_1/Hetero_fmn_complex/1'>TextToBeDisplayed</scene> | <scene name='User:Mitchell_Long/Sandbox_1/Hetero_fmn_complex/1'>TextToBeDisplayed</scene> | ||
==Structural Motifs== | ==Structural Motifs== | ||
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<p>Active Site and Alpha Subunit-the <scene name='User:Mitchell_Long/Sandbox_1/Yellow_sheets/1'>flavin binding pocket</scene> of bacterial luciferase is a large open cavity that is accessible to solvent via an opening located at the C-terminal ends of the ǰ strans of the TIM-barrel structure. During the first step of the oxidation reaction, FMNH<sub>2</sub> binds to the flavin binding pocket and the enzyme undergoes a conformational change that blocks water in the surrounding environment from accessing both the excited peroxydihydroflavin intermediate. Next O<sub>2</sub> and a long chain aldehyde bind to the FMNH<sub>2</sub> luciferase complex and a two step oxidatino reaction occurs. | <p>Active Site and Alpha Subunit-the <scene name='User:Mitchell_Long/Sandbox_1/Yellow_sheets/1'>flavin binding pocket</scene> of bacterial luciferase is a large open cavity that is accessible to solvent via an opening located at the C-terminal ends of the ǰ strans of the TIM-barrel structure. During the first step of the oxidation reaction, FMNH<sub>2</sub> binds to the flavin binding pocket and the enzyme undergoes a conformational change that blocks water in the surrounding environment from accessing both the excited peroxydihydroflavin intermediate. Next O<sub>2</sub> and a long chain aldehyde bind to the FMNH<sub>2</sub> luciferase complex and a two step oxidatino reaction occurs. | ||
.</p> | .</p> | ||
<scene name='User:Mitchell_Long/Sandbox_1/Hetero_translucent/1'>Heterodimer</scene> | |||
<scene name='User:Mitchell_Long/Sandbox_1/Fmn_in_barrel/1'>FMN bound Heterodimer</scene> | |||
<p>The β subunit-The beta subunit is characterized as a necessary but non-catalytic subunit that stabilizes the catalytic ǯ subunit that is responsible for the oxidation reaction. Both subunits share a great deal of homology | <p>The β subunit-The beta subunit is characterized as a necessary but non-catalytic subunit that stabilizes the catalytic ǯ subunit that is responsible for the oxidation reaction. Both subunits share a great deal of homology | ||
