Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Crystallization (Commentary)

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 5 of 5
EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.3- 348568
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.3apo-enzyme, to 1.85 A resolution. Apo-LuxF possesses four preorganized binding sites for 6-(3'-(R)-myristyl)-FMN 744404
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.3bacterial luciferase/FMN complex, by the hanging drop method, at 2.3 A resolution. Crystals of recombinant luciferase are grown at room temperature prior to soaking with millimolar concentrations of FMN. Belongs to space group P212121. The isoalloxazine ring is coordinated by an unusual cis-Ala-Ala peptide bond. The reactive sulfhydryl group of Cys106 projects toward position C-4a, the site of flavin oxygenation. Mobile loop that is crystallographically disordered, appears to be a boundary between solvent and the active center. Within this portion of the protein, there is a single contact between Phe272 of the R subunit and Tyr151 of the beta subunit 702318
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.3comparison of the conformational transitions of luciferases from Vibrio harveyi and Photobacterium leiognathi during equilibrium unfolding with urea. Vibrio harveyi luciferase in its native state demonstrates a higher fluorescence intensity per one protein molecule, but a shorter fluorescence lifetime, than Photobacterium leiognathi luciferase. During the first stage of denaturation (at more than 2 M of urea), for V. harveyi luciferase, the fluorescence lifetimes tau1 and tau2 show an increase, while for the P. leiognathi enzyme, the lifetime components decrease. This stage includes the unfolding of the C-terminal domain of the luciferase alpha-subunit. Subunit dissociation does not influence the optical characteristics of either of the luciferases. The unfolding of the subunits occurs in the same way for the two proteins 764918
Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.3structure is determined in absence of substrate at low-salt concentrations 348610
Results 1 - 5 of 5