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Bioluminescence Is Produced from a Trapped Firefly Luciferase Conformation Predicted by the Domain Alternation Mechanism

Branchini, Bruce R ; Rosenberg, Justin C ; Fontaine, Danielle M ; Southworth, Tara L ; Behney, Curran E ; Uzasci, Lerna

Journal of the American Chemical Society, 2011-07, Vol.133 (29), p.11088-11091 [Periódico revisado por pares]

United States: American Chemical Society

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Título:
Bioluminescence Is Produced from a Trapped Firefly Luciferase Conformation Predicted by the Domain Alternation Mechanism
Autor: Branchini, Bruce R ; Rosenberg, Justin C ; Fontaine, Danielle M ; Southworth, Tara L ; Behney, Curran E ; Uzasci, Lerna
Assuntos: Amino Acid Sequence ; Animals ; Fireflies - enzymology ; Fireflies - genetics ; Fireflies - metabolism ; Firefly Luciferin - metabolism ; Luciferases, Firefly - chemistry ; Luciferases, Firefly - genetics ; Luciferases, Firefly - metabolism ; Luminescence ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Structure, Tertiary
É parte de: Journal of the American Chemical Society, 2011-07, Vol.133 (29), p.11088-11091
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: According to the domain alternation mechanism and crystal structure evidence, the acyl-CoA synthetases, one of three subgroups of a superfamily of adenylating enzymes, catalyze adenylate- and thioester-forming half-reactions in two different conformations. The enzymes accomplish this by presenting two active sites through an ∼140° rotation of the C-domain. The second half-reaction catalyzed by another subgroup, the beetle luciferases, is a mechanistically dissimilar oxidative process that produces bioluminescence. We have demonstrated that a firefly luciferase variant containing cysteine residues at positions 108 and 447 can be intramolecularly cross-linked by 1,2-bis(maleimido)ethane, trapping the enzyme in a C-domain-rotated conformation previously undocumented in the available luciferase crystal structures. The cross-linked luciferase cannot adenylate luciferin but is nearly fully capable of bioluminescence with synthetic luciferyl adenylate because it retains the ability to carry out the oxidative half-reaction. The cross-linked luciferase is apparently trapped in a conformation similar to those adopted by acyl-CoA synthetases as they convert acyl adenylates into the corresponding CoA thioesters.
Editor: United States: American Chemical Society
Idioma: Inglês

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Bioluminescence Is Produced from a Trapped Firefly Luciferase Conformation Predicted by the Domain Alternation Mechanism

Branchini, Bruce R ; Rosenberg, Justin C ; Fontaine, Danielle M ; Southworth, Tara L ; Behney, Curran E ; Uzasci, Lerna

United States: American Chemical Society

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