Sandbox 167: Difference between revisions
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== Structure == | == 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 />. | 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>. | ||
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="main" />. | 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="main" />. | ||
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Notes about the image | Notes about the image | ||