Sandbox 167: Difference between revisions

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Andrea Gorrell, James Jones

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 == Structure ==
-Chemically, L. cruciata luciferase  is similiar to aminoacyl-tRNA synthetases, so much that DLSA, an analog of a potent inhibitor of said synthetases was used to help solve it's structure. While the primary sequence of both proteins is similiar, the binding affinity of the luciferase for this inhibitor also suggests that the first part of the luciferase reaction might share a similiar mechanism as well. <ref name="structure">PMID:16541080 </ref>.
+Generally, firefly luciferases have some similarities with Acyl-CoA ligases and some peptide synthetases despite having different cellular effects. In fixing the structure of L. cruciata luciferase, the analog of a potent aminoacyl-tRNA synthetases (DLSA) was successfuly utilized to represent a stable oxyluciferin intermediate.<ref name="structure">PMID:16541080 </ref>.
-The active site for this luciferase lies within a central area of the protein, and is composed of an α-helix (residues 248-260) and four short β-sheets (residues 286-289, 313-316, 339-342 and 351-353. Ile288 has been implicated as an important residue in determining the hydrophobicity of the active site environment, and through orientation of the product oxyluciferin, the bioluminescent colour. <ref name="structure" />.
+The DLSA occupied the active site of the luciferase, which is composed of an α-helix (residues 248-260) and four short β-sheets (residues 286-289, 313-316, 339-342 and 351-353. Ile288 has been implicated as an important residue in determining the hydrophobicity of the active site environment, and through orientation of the product oxyluciferin, the bioluminescent colour. <ref name="structure" />.
 [[Image:2d1s active site with ILE288.jpg | thumb |none | upright=3.0 | Figure 1: PYMOL image of 2D1S highlighting active site and Ile288, putatively identified in hydrophobic control of bioluminescent colour.]]