User:Mitchell Long/Sandbox 1: Difference between revisions
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==Introduction== | ==Introduction== | ||
Luciferases are a class of enzymes that catalyze the oxidation of a long chain aliphatic aldehydes. This reaction results in the formation of a carboxylic acid and the emission of photons in the form of blue-green light. The luciferase found in ''''Vibrio harveyi'''' is a heterodimer that is composed of a catalytic α subunit and a homologous but noncatalytic β subunit. The catalytic α subunit houses the FMN cofactor and is connected to the β subunit via a hairpin structure called the "mobile loop." | Luciferases are a class of enzymes that catalyze the oxidation of a long chain aliphatic aldehydes. This reaction results in the formation of a carboxylic acid and the emission of photons in the form of blue-green light. The luciferase found in ''''Vibrio harveyi'''' is a heterodimer that is composed of a catalytic α subunit and a homologous but noncatalytic β subunit. The catalytic α subunit houses the FMN cofactor and is connected to the β subunit via a hairpin structure called the "mobile loop." | ||
==Structural Motifs== | |||
Structure homology-There is a great deal of sequence homology and structural coservation between the α and β subunits. When superimposed over eachother the barrels of the alpha and beta subunits with a deviation of 0.62Å for 42 equivalent | |||
α carbons. The region of the beta subunit that contains the 29 residue deletion with respect to the alpha subunit differs notably in arrangement. In the alpha subunit, the α7a helix is straight and extens toward the beta subunit. the region involved with dimerization, helices ǯ and β and the hairpin loop structure are exceptionally similar in superposition. | |||
==Mechanism== | |||
Luciferase found in'''V. Harveyi''' binds noncovalently to a reduced flavin mononucleotide cofactor, an aliphatic aldehyde and oxygen to yield oxidized flavin mononucleotide, water, and carboxylic acid. The reaction occurs in two steps forming a hydroxyflavin intermediate and ultimately results in the oxidation of the aldehyde and emission of photons in the form of blue green light. | |||
<p>FMNH<sub>2</sub>+O<sub>2</sub>+RCHO→FMN+RCOOH+H<sub>2</sub>O+hv(490nm)</p> | |||
The catalytic α subunit houses the FMN cofactor and is connected to the β subunit via a hairpin structure called the "mobile loop." The organic substrate for bacterial luciferase in vivo is myristic aldehyde, although many aliphatic aldehydes of various lengths can induce bioluminescence in vitro. | |||
==Structural Motifs== | ==Structural Motifs== | ||
Structure homology-There is a great deal of sequence homology and structural coservation between the α and β subunits. When superimposed over eachother the barrels of the alpha and beta subunits with a deviation of 0.62Å for 42 equivalent | <p>Structure homology-There is a great deal of sequence homology and structural coservation between the α and β subunits. When superimposed over eachother the barrels of the alpha and beta subunits with a deviation of 0.62Å for 42 equivalent | ||
α carbons. The region of the beta subunit that contains the 29 residue deletion with respect to the alpha subunit differs notably in arrangement. In the alpha subunit, the α7a helix is straight and extens toward the beta subunit. the region involved with dimerization, helices &# | α carbons. The region of the beta subunit that contains the 29 residue deletion with respect to the alpha subunit differs notably in arrangement. In the alpha subunit, the α7a helix is straight and extens toward the beta subunit. the region involved with dimerization, helices ǯ and β and the hairpin loop structure are exceptionally similar in superposition. </p> | ||
<p>Active Site | <p>Active Site | ||
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(β/α)<SUB>8</SUB> Barrel- The tertiary structure of the α and β subunits is very similar. both subunits fold into a single-domain eight-stranded β/α 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. | (β/α)<SUB>8</SUB> Barrel- The tertiary structure of the α and β subunits is very similar. both subunits fold into a single-domain eight-stranded β/α 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. | ||
.</p> | .</p> | ||
</StructureSection> | |||
{{STRUCTURE_3fgc| PDB=3fgc | SCENE= }} | |||
Subunit Homology-the topology of the αand β subunits is identical. In the alpha subnunit, the γ7-α7 loop is 71 residues long and contains 29 residues not present in the beta subunit. | Subunit Homology-the topology of the αand β subunits is identical. In the alpha subnunit, the γ7-α7 loop is 71 residues long and contains 29 residues not present in the beta subunit. | ||
