User:Mitchell Long/Sandbox 1: Difference between revisions
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==Mechanism of Bio luminescence== | ==Mechanism of Bio luminescence== | ||
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." | 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." 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 | 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. | 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 ⓬ and ⓭ and the hairpin loop structure are exceptionally similar in superposition. | ||
Mobile Loop- Phe2772-thr 288 | <p>Active Site | ||
(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>Mobile Loop- Phe2772-thr 288 | |||
(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. | |||
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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. | ||