4NC4

Crystal structure of photoreceptor AtUVR8 mutant W285F and light-induced structural changes at 120K

Summary for 4NC4

• Entry DOI: 10.2210/pdb4nc4/pdb
• Related: 4NAA 4NC4
• Descriptor: Ultraviolet-B receptor UVR8, MAGNESIUM ION (3 entities in total)
• Functional Keywords: 7-blade beta-propeller, signaling protein
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Nucleus: Q9FN03
• Total number of polymer chains: 4
• Total formula weight: 163783.08

Authors

Yang, X.,Zeng, X.,Zhao, K.-H.,Ren, Z. (deposition date: 2013-10-23, release date: 2016-10-26, Last modification date: 2023-09-20)

Primary citation

Zeng, X.,Ren, Z.,Wu, Q.,Fan, J.,Peng, P.P.,Tang, K.,Zhang, R.,Zhao, K.H.,Yang, X.
Dynamic Crystallography Reveals Early Signalling Events in Ultraviolet Photoreceptor UVR8.
Nat Plants, 1:-, 2015

PubMed Abstract: UVR8 (UVR8) is a long-sought-after photoreceptor that undergoes dimer dissociation in response to UV-B light. Crystallographic and mutational studies have identified two crucial tryptophan residues for UV-B responses in UVR8. However, the mechanism of UV-B perception and structural events leading up to dimer dissociation remain elusive at the molecular level. We applied dynamic crystallography to capture light-induced structural events in photoactive UVR8 crystals. Here we report two intermediate structures at 1.67Å resolution. At the epicenter of UV-B signaling, concerted motions associated with Trp285/Trp233 lead to ejection of a water molecule, which weakens an intricate network of hydrogen bonds and salt bridges at the dimer interface. Partial opening of the β-propeller structure due to thermal relaxation of conformational strains originating in the epicenter further disrupts the dimer interface and leads to dimer dissociation. These dynamic crystallographic observations provide structural insights into the photo-perception and signaling mechanism of UVR8.

PubMed: 26097745
DOI: 10.1038/nplants.2014.6

Experimental method

X-RAY DIFFRACTION (1.75 Å)