6Q2M
Crystal structure of Photinus pyralis Luciferase Pps6 mutant in complex with DLSA
Summary for 6Q2M
| Entry DOI | 10.2210/pdb6q2m/pdb |
| Related | 4G36 |
| Descriptor | Luciferin 4-monooxygenase, SULFATE ION, (2S,5S)-hexane-2,5-diol, ... (6 entities in total) |
| Functional Keywords | luciferase, adenylation domain, ligase, bioluminescence |
| Biological source | Photinus pyralis (Common eastern firefly) |
| Total number of polymer chains | 3 |
| Total formula weight | 188992.87 |
| Authors | Patel, K.D.,Gulick, A.M. (deposition date: 2019-08-08, release date: 2019-10-16, Last modification date: 2023-10-11) |
| Primary citation | Branchini, B.R.,Fontaine, D.M.,Southworth, T.L.,Huta, B.P.,Racela, A.,Patel, K.D.,Gulick, A.M. Mutagenesis and Structural Studies Reveal the Basis for the Activity and Stability Properties That Distinguish thePhotinusLuciferasesscintillansandpyralis. Biochemistry, 58:4293-4303, 2019 Cited by PubMed Abstract: The dazzling yellow-green light emission of the common North American firefly and other bioluminescent organisms has provided a wide variety of prominent research applications like reporter gene assays and in vivo imaging methods. While the enzyme has been extensively studied, only recently has a second luciferase been cloned from the species . Even though the enzymes share very high sequence identity (89.8%), the color of the light they emit, their specific activity and their stability to heat, pH, and chemical denaturation are quite different with the luciferase being generally more resistant. Through the construction and evaluation of the properties of chimeric domain swapped, single point, and various combined variants, we have determined that only six amino acid changes are necessary to confer all of the properties of the enzyme to wild-type luciferase. Altered stability properties were attributed to four of the amino acid changes (T214N/S276T/H332N/E354N), and single mutations each predominantly changed emission color (Y255F) and specific activity (A222C). Results of a crystallographic study of the enzyme containing the six changes (Pps6) provide some insight into the structural basis for some of the documented property differences. PubMed: 31560532DOI: 10.1021/acs.biochem.9b00719 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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