Not as easy as π: An insertional residue does not explain the π-helix gain-of-function in two-component FMN reductases

Protein Science : a Publication of the Protein Society
Jeffrey S McFarlaneHolly R Ellis

Abstract

The π-helix located at the tetramer interface of two-component FMN-dependent reductases contributes to the structural divergence from canonical FMN-bound reductases within the NADPH:FMN reductase family. The π-helix in the SsuE FMN-dependent reductase of the alkanesulfonate monooxygenase system has been proposed to be generated by the insertion of a Tyr residue in the conserved α4-helix. Variants of Tyr118 were generated, and their X-ray crystal structures determined, to evaluate how these alterations affect the structural integrity of the π-helix. The structure of the Y118A SsuE π-helix was converted to an α-helix, similar to the FMN-bound members of the NADPH:FMN reductase family. Although the π-helix was altered, the FMN binding region remained unchanged. Conversely, deletion of Tyr118 disrupted the secondary structural properties of the π-helix, generating a random coil region in the middle of helix 4. Both the Y118A and Δ118 SsuE SsuE variants crystallize as a dimer. The MsuE FMN reductase involved in the desulfonation of methanesulfonates is structurally similar to SsuE, but the π-helix contains a His insertional residue. Exchanging the π-helix insertional residue of each enzyme did not result in equivalent kinetic proper...Continue Reading

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Citations

Dec 18, 2019·Organic & Biomolecular Chemistry·Sergio Di SilvioGennaro Pescitelli
Aug 6, 2019·Current Opinion in Structural Biology·Lejla Zubcevic, Seok-Yong Lee

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