7ph0
Structure of light-adapted AsLOV2 Q513L
Structural highlights
FunctionPublication Abstract from PubMedIn nature as in biotechnology, light-oxygen-voltage photoreceptors perceive blue light to elicit spatiotemporally defined cellular responses. Photon absorption drives thioadduct formation between a conserved cysteine and the flavin chromophore. An equally conserved, proximal glutamine processes the resultant flavin protonation into downstream hydrogen-bond rearrangements. Here, we report that this glutamine, long deemed essential, is generally dispensable. In its absence, several light-oxygen-voltage receptors invariably retained productive, if often attenuated, signaling responses. Structures of a light-oxygen-voltage paradigm at around 1 A resolution revealed highly similar light-induced conformational changes, irrespective of whether the glutamine is present. Naturally occurring, glutamine-deficient light-oxygen-voltage receptors likely serve as bona fide photoreceptors, as we showcase for a diguanylate cyclase. We propose that without the glutamine, water molecules transiently approach the chromophore and thus propagate flavin protonation downstream. Signaling without glutamine appears intrinsic to light-oxygen-voltage receptors, which pertains to biotechnological applications and suggests evolutionary descendance from redox-active flavoproteins. Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine.,Dietler J, Gelfert R, Kaiser J, Borin V, Renzl C, Pilsl S, Ranzani AT, Garcia de Fuentes A, Gleichmann T, Diensthuber RP, Weyand M, Mayer G, Schapiro I, Moglich A Nat Commun. 2022 May 12;13(1):2618. doi: 10.1038/s41467-022-30252-4. PMID:35552382[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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