Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism.

摘要: Beetle luciferases catalyze a two-step reaction that includes the initial adenylation of luciferin substrate, followed by an oxidative decarboxylation ultimately produces light. Evidence for homologous acyl-CoA synthetases supports domain alternation catalytic mechanism in which these enzymes’ C-terminal rotates ∼140° to adopt two conformations are used partial reactions. While many structures exist both conformations, date only biochemical evidence with luciferase. We have determined structure cross-linked luciferase enzyme is trapped second conformation. This new role conformation and provides insights into step.