2RH7

Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla Reniformis

Replaces:  2PSL

Summary for 2RH7

• Entry DOI: 10.2210/pdb2rh7/pdb
• Descriptor: Green fluorescent protein (2 entities in total)
• Functional Keywords: fluorescent protein
• Biological source: Renilla reniformis
• Total number of polymer chains: 4
• Total formula weight: 108243.44

Authors

Loening, A.M.,Fenn, T.D.,Gambhir, S.S. (deposition date: 2007-10-06, release date: 2007-10-23, Last modification date: 2023-11-15)

Primary citation

Loening, A.M.,Fenn, T.D.,Gambhir, S.S.
Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla reniformis.
J.Mol.Biol., 374:1017-1028, 2007

PubMed 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.

PubMed: 17980388
DOI: 10.1016/j.jmb.2007.09.078

Experimental method

X-RAY DIFFRACTION (1.5 Å)