Luciola cruciata luciferase: Difference between revisions

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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" />.
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" />.
{{STRUCTURE_2d1s|  PDB=2d1s  ||SIZE=400|  SCENE=Luciferase/2d1s/2  |CAPTION= 2d1s, resolution 1.30&Aring; (<scene name='Luciferase/2d1s/2'>default scene</scene>). }}


==Spectral difference with mutated luciferases==
==Spectral difference with mutated luciferases==