2rh7
From Proteopedia
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Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla Reniformis
Overview
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.
About this Structure
2RH7 is a Single protein structure of sequence from Renilla reniformis. This structure superseeds the now removed PDB entry 2PSL. Full crystallographic information is available from OCA.
Reference
Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis., Loening AM, Fenn TD, Gambhir SS, J Mol Biol. 2007 Dec 7;374(4):1017-28. Epub 2007 Oct 3. PMID:17980388
Page seeded by OCA on Wed Jan 23 11:57:46 2008
