Sandbox Reserved 993: Difference between revisions
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[[Image:Screenshot_2015-02-22_22.56.09.png|alt text]]<ref>Auld, D.S., Southhall, N. T., Jadhav, A., Johnson, R. L., Diller, D. J., Simeonov, A., Austin, C. P., and Inglese, J. (2008) "Characteristics of chemical libraries for luciferase inhibitory activity", J. Med. Chem. 51(8):2372-2386. doi:10.1021/jm701302v</ref> | [[Image:Screenshot_2015-02-22_22.56.09.png|alt text]]<ref>Auld, D.S., Southhall, N. T., Jadhav, A., Johnson, R. L., Diller, D. J., Simeonov, A., Austin, C. P., and Inglese, J. (2008) "Characteristics of chemical libraries for luciferase inhibitory activity", J. Med. Chem. 51(8):2372-2386. doi:10.1021/jm701302v</ref> | ||
== Structure == | == Structure == | ||
''Photinus pyralis'' luciferase is composed of 550 residues, resulting in a 62 kDa molecular weight. The protein is divided into two domains (the N-terminal domain and the C-terminal domain) by a wide cleft. The N-terminal domain (residues 4-436) is much larger than the C-terminal domain (residues 440-544) and is formed by an antiparallet β-barrel, two β-sheets, and two α-helices. <ref>Conti E., Franks N.P., Brick P. (1996) "Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes", Structure 4(3): 287-298.</ref> | |||
== Lab Use == | == Lab Use == | ||
