Loening_2007_J.Mol.Biol_374_1017

Reference

Title : Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis - Loening_2007_J.Mol.Biol_374_1017
Author(s) : Loening AM , Fenn TD , Gambhir SS
Ref : Journal of Molecular Biology , 374 :1017 , 2007
Abstract : Due to its ability to emit light, the luciferase from Renilla reniformis (RLuc) is widely employed in molecular biology as a reporter gene in cell culture experiments and small animal imaging. To accomplish this bioluminescence, the 37-kDa enzyme catalyzes the degradation of its substrate coelenterazine in the presence of molecular oxygen, resulting in the product coelenteramide, carbon dioxide, and the desired photon of light. We successfully crystallized a stabilized variant of this important protein (RLuc8) and herein present the first structures for any coelenterazine-using luciferase. These structures are based on high-resolution data measured to 1.4 A and demonstrate a classic alpha/beta-hydrolase fold. We also present data of a coelenteramide-bound luciferase and reason that this structure represents a secondary conformational form following shift of the product out of the primary active site. During the course of this work, the structure of the luciferase's accessory green fluorescent protein (RrGFP) was also determined and shown to be highly similar to that of Aequorea victoria GFP.
ESTHER : Loening_2007_J.Mol.Biol_374_1017
PubMedSearch : Loening_2007_J.Mol.Biol_374_1017
PubMedID: 17980388
Gene_locus related to this paper: renre-luc

Related information

Gene_locus related to this paper: renre-luc

Citations formats

Loening AM, Fenn TD, Gambhir SS (2007)
Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis
Journal of Molecular Biology 374 :1017

Loening AM, Fenn TD, Gambhir SS (2007)
Journal of Molecular Biology 374 :1017