Bacterial luciferase structure

Baldwin, T. O., etal. (1987). Structural studies of bacterial luciferases results from recombinant DNA technology. In Schoelmerich, J. (ed.), Biolumin. Chemilumin., Proc. Int. Biolumin. Chemilumin. Symp., 4th, 1986, pp. 351-360. Wiley, Chichester, UK. 

Fisher, A. J., Raushel, F. M., Baldwin, T. O., and Rayment, I. (1995). Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 A resolution. Biochemistry 34 6581-6586. 

Hastings, J. W., et al. (1969a). Structurally distinct bacterial luciferase. Biochemistry 8 4681-4689. 

Sinclair, J. F., Waddle, J. J., Waddill, E. F., and Baldwin, T. O. (1993). Purified native subunits of bacterial luciferase are active in the bioluminescence reaction but fail to assemble into the a(3 structure. Biochemistry 32 5036-5044. 

Bacterial bioluminescence, 30-46 factors required, 31 general scheme, 32 in vivo luminescence, 41 luminescence reaction, 37, 38 Bacterial luciferase, 33-35, 343 assay, 39 cloning, 34 crystal structure, 34 extraction and purification, 34 inactivation, 34, 35 molecular weight, 34 properties, 34 storage, 35 subunits, 34... 

Tanner J, Mitchell D, Tu S-C, Miller S. Structure of bacterial luciferase homodimer Implications for flavin binding. Biochem 1997 36 665-72. 

Bacterial luciferase is a heterodimer (75 kDa). The connection to the substrate is realized by the a-subunit (40 kDa), while the P-subunit (35 kDa) assures the stability of the active dimmer-structure. The luciferase molecule has active highly specific connection centers for FMN2, FMN, AMP and aldehyde [11]. 

The firefly enzyme might have its own problem by the fact that it is localized in vivo (yeast, mammalian, and plant cells as in the firefly lantern) in small vesicular structures called peroxisomes (55). This is due to the presence of a peroxisomal translocation signal located at the C-terminal domain of the molecule. The peroxisomal localization may present an additional membrane barrier for in situ detection of the enzyme, although it offers a particular advantage for studying protein transport or targeting to peroxisomes. Removal of the peroxisomal translocation signal has been shown to provide an alternative system in which the modified firefly luciferase is expressed as a cytoplasmic enzyme like bacterial luciferases. 

Tu, S. Wu, C. Hastings, J. W. Structural studies on bacterial luciferase using energy transfer and emission aiusotropy. Biochemistry 1978, 77, 987-993. 

Kurfiirst, M., Ghisla, S., and Hastings, J.W., Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction, Proc. Natl. Acad. Sci. USA, 81, 2990,1984. 

Thoden, J.B., Holden, H.M., Fisher, A.J., Sinclair, J.F., Wesenberg, G., Baldwin, TO., and Rayment, 1., Structure of the Pj homodimer of bacterial luciferase from Vibrio harveyi x-ray anal) is of a kinetic protein folding trap. Protein Sci., 6, 13,1997. 

Lin, L.Y., Sulea, T, Szittner, R., Vassilyev, V, Purisima, E.O., and Meighen, E.A., Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data. Protein ScL, 10, 1563, 2001. 

An important phenomenon, now called quorum sensing, was discovered from studies of bacterial bioluminescence, in which it was found that growth and luminescence are controlled separately.22 After inoculating a culture into fresh medium, growth is exponential with no lag, but the amount of luciferase remains constant for the first three hours, after which its synthesis and light emission increase very, very rapidly (Fig. 6). This was shown to be due to the production and release into the medium of a substance that we named autoinducer upon reaching a critical concentration, it induces the synthesis of luciferase and other proteins involved in the bioluminescence. Eberhard and colleagues determined the structure to be a homoserine lactone and synthesized it.23... 

Bacterial L. has not yet been characterized. The corresponding luciferase produces luminescence in the presence of FMNH and straight chain aldehydes with more than 7 C-atoms. Structural elucidation of L. was delayed on account of their low natural concentration. 30,000 fireflies were required for the isolation of IS mg L., and 40,000 sea pansies yielded only O.S mg of the Renitla L. Many L. and synthetic analogs show a spontaneous luminescence in proton-free solvents, such as dimethyl sulfoxide, but the quantum yield is lower than in bioluminescence. See also Photoproteins. 

Luciferin includes a whole family of compounds whose heterocyclic structures vary fix>m one organism to another. Most luciferase enzymes use the same cofactors as metabolic processes (ATP, FMN, NADH), and bioluminescence is easily associated with other types of Inological reactions for analytical applications. Firefly ludferase is used tt> follow processes that use adenosine triphosphate (ATP) as a cofactor, for example, the measurement of biomass, the detection of a bacterial infection, antibiotic assays, and the monitoring of other enzymatic reactions that consume or produce ATP. Luciferase catalyses all these reactions according to the following overall reaction scheme ... 

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