Journal
BIOCHEMISTRY
Volume 51, Issue 33, Pages 6493-6495Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi300934s
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Funding
- National Science Foundation [MCB0842831]
- Air Force Office of Scientific Research [FA9550-10-1-0174]
- Hans & Ella McCollum '21 Vahlteich Endowment
- National Institute of General Medical Science of the National Institutes of Health [GM-068440]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0842831] Funding Source: National Science Foundation
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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 similar to 140 degrees 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 crosslinked 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 biochemical mechanism of the luciferase oxidative step.
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