Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2PSE

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

Summary for 2PSE
Entry DOI10.2210/pdb2pse/pdb
Related2PSD 2PSF 2PSH 2PSJ 2PSL
DescriptorRenilla-luciferin 2-monooxygenase, IMIDAZOLE (3 entities in total)
Functional Keywordsalpha/beta-hydrolase, luciferase, oxidoreductase
Biological sourceRenilla reniformis
Total number of polymer chains1
Total formula weight37069.26
Authors
Loening, A.M.,Fenn, T.D.,Gambhir, S.S. (deposition date: 2007-05-06, release date: 2007-05-22, Last modification date: 2024-02-21)
Primary citationLoening, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon