Structural highlights
Function
A0A140UHJ0_PHATR
Publication Abstract from PubMed
Light-oxygen-voltage (LOV) domains absorb blue light for mediating various biological responses in all three domains of life. Aureochromes from stramenopile algae represent a subfamily of photoreceptors that differs by its inversed topology with a C-terminal LOV sensor and an N-terminal effector (basic region leucine zipper, bZIP) domain. We crystallized the LOV domain including its flanking helices, A'alpha and Jalpha, of aureochrome 1a from Phaeodactylum tricornutum in the dark state and solved the structure at 2.8 A resolution. Both flanking helices contribute to the interface of the native-like dimer. Small-angle X-ray scattering shows light-induced conformational changes limited to the dimeric envelope as well as increased flexibility in the lit state for the flanking helices. These rearrangements are considered to be crucial for the formation of the light-activated dimer. Finally, the LOV domain of the class 2 aureochrome PtAUREO2 was shown to lack a chromophore because of steric hindrance caused by M301.
Structure of a Native-like Aureochrome 1a LOV Domain Dimer from Phaeodactylum tricornutum.,Banerjee A, Herman E, Kottke T, Essen LO Structure. 2016 Jan 5;24(1):171-8. doi: 10.1016/j.str.2015.10.022. Epub 2015 Dec , 10. PMID:26688213[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Banerjee A, Herman E, Kottke T, Essen LO. Structure of a Native-like Aureochrome 1a LOV Domain Dimer from Phaeodactylum tricornutum. Structure. 2016 Jan 5;24(1):171-8. doi: 10.1016/j.str.2015.10.022. Epub 2015 Dec , 10. PMID:26688213 doi:http://dx.doi.org/10.1016/j.str.2015.10.022
