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

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

SUBMITTER: Sundlov JA 

PROVIDER: S-EPMC3425952 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature