Crystal Structures of Aureochrome1 LOV Suggest New Design Strategies for Optogenetics

Journal Article · Thu Oct 02 04:00:00 EDT 2014 · Structure

DOI:https://doi.org/10.1016/j.str.2012.02.016· OSTI ID:1038286

Mitra, Devrani; Yang, Xiaojing; Moffat, Keith ^[1]

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1. UC

Aureochrome1, a signaling photoreceptor from a eukaryotic photosynthetic stramenopile, confers blue-light-regulated DNA binding on the organism. Its topology, in which a C-terminal LOV sensor domain is linked to an N-terminal DNA-binding bZIP effector domain, contrasts with the reverse sensor-effector topology in most other known LOV-photoreceptors. How, then, is signal transmitted in Aureochrome1? The dark- and light-state crystal structures of Aureochrome1 LOV domain (AuLOV) show that its helical N- and C-terminal flanking regions are packed against the external surface of the core {beta} sheet, opposite to the FMN chromophore on the internal surface. Light-induced conformational changes occur in the quaternary structure of the AuLOV dimer and in Phe298 of the H{beta} strand in the core. The properties of AuLOV extend the applicability of LOV domains as versatile design modules that permit fusion to effector domains via either the N- or C-termini to confer blue-light sensitivity.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: NIH
• OSTI ID: 1038286
• Journal Information: Structure, Journal Name: Structure Journal Issue: (4) ; 04, 2012 Vol. 20
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
CONFORMATIONAL CHANGES
CRYSTAL STRUCTURE
DESIGN
DIMERS
DNA
SENSITIVITY
SENSORS
TOPOLOGY