Luciferase FMN complex- Vibrio harveyi: Difference between revisions

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<p>'''Structure homology'''-There is a great deal of sequence homology and structural coservation between the &#945; and &#946; subunits.  When superimposed over  the barrels of the alpha and beta subunits with a deviation of 0.62&#197; for 42 equivalent &#945; carbons. The region of the beta subunit that contains the 29 residue deletion with respect to the alpha subunit differs notably in arrangement<ref name=Fisher, A.J.>PMID: 7756289</ref> .  In the alpha subunit, the &#945;7a helix is straight and extends toward the beta subunit.  The region involved with dimerization, helices &#945; and &#946; are exceptionally similar in superposition.  
<p>'''Structure homology'''-There is a great deal of sequence homology and structural coservation between the &#945; and &#946; subunits.  When superimposed over  the barrels of the alpha and beta subunits with a deviation of 0.62&#197; for 42 equivalent &#945; carbons. The region of the beta subunit that contains the 29 residue deletion with respect to the alpha subunit differs notably in arrangement<ref name=Fisher, A.J.>PMID: 7756289</ref> .  In the alpha subunit, the &#945;7a helix is straight and extends toward the beta subunit.  The region involved with dimerization, helices &#945; and &#946; are exceptionally similar in superposition.  
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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 &#496; strands of the TIM-barrel structure<ref Campbell, Z.T.>PMID: 19435287</ref>.   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 &#496; strands of the TIM-barrel structure<ref Campbell, Z.T.>PMID: 19435287</ref>.   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. This blocks water from the surrounding environment from attacking 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 oxidation reaction occurs<ref Campbell, Z.T.>PMID: 19435287</ref>.   
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<scene name='User:Mitchell_Long/Sandbox_1/Hetero_translucent/1'>Heterodimer</scene>
<scene name='User:Mitchell_Long/Sandbox_1/Hetero_translucent/1'>Heterodimer</scene>
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(&#946;/&#945;)<SUB>8</SUB> TIM Barrel- The tertiary structure of the &#945; and &#946; subunits is very similar.  While both the alpha and beta subunits are similar, the alpha subunit contains an extra 29 residues that the beta lacks.  Both subunits fold into a single-domain eight-stranded &#946;/&#945; barrel motif.  the two subunits assemble around a parallel four-helix bundle centered on a pseudo 2-fold axis that relates the alpha and beta subunits<ref Campbell, Z.T.>PMID: 19435287</ref>.  
(&#946;/&#945;)<SUB>8</SUB> TIM Barrel- The tertiary structure of the &#945; and &#946; subunits are very similar, except the alpha subunit contains an extra 29 residues that the beta lacks.  These 29 subunits make up the mobile loop.  Both subunits fold into a single-domain eight-stranded &#946;/&#945; barrel motif.  the two subunits assemble around a parallel four-helix bundle centered on a pseudo 2-fold axis that relates the alpha and beta subunits<ref Campbell, Z.T.>PMID: 19435287</ref>.  
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</StructureSection>
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Mitchell Long, Michal Harel, Loïc Gazquez
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