4D9S

Crystal structure of Arabidopsis thaliana UVR8 (UV Resistance locus 8)

4D9S の概要

• エントリーDOI: 10.2210/pdb4d9s/pdb
• 分子名称: UVB-resistance protein UVR8 (2 entities in total)
• 機能のキーワード: uv resistance, uv-b photoreceptor, tryptophan chromophores, homodimer, cop1, chromatin-binding protein
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87102.48

構造登録者

Arvai, A.S.,Christie, J.M.,Pratt, A.J.,Hitomi, K.,Getzoff, E.D. (登録日: 2012-01-11, 公開日: 2012-04-04, 最終更新日: 2023-09-13)

主引用文献

Christie, J.M.,Arvai, A.S.,Baxter, K.J.,Heilmann, M.,Pratt, A.J.,O'Hara, A.,Kelly, S.M.,Hothorn, M.,Smith, B.O.,Hitomi, K.,Jenkins, G.I.,Getzoff, E.D.
Plant UVR8 Photoreceptor Senses UV-B by Tryptophan-Mediated Disruption of Cross-Dimer Salt Bridges.
Science, 335:1492-1496, 2012

PubMed Abstract: The recently identified plant photoreceptor UVR8 (UV RESISTANCE LOCUS 8) triggers regulatory changes in gene expression in response to ultraviolet-B (UV-B) light through an unknown mechanism. Here, crystallographic and solution structures of the UVR8 homodimer, together with mutagenesis and far-UV circular dichroism spectroscopy, reveal its mechanisms for UV-B perception and signal transduction. β-propeller subunits form a remarkable, tryptophan-dominated, dimer interface stitched together by a complex salt-bridge network. Salt-bridging arginines flank the excitonically coupled cross-dimer tryptophan "pyramid" responsible for UV-B sensing. Photoreception reversibly disrupts salt bridges, triggering dimer dissociation and signal initiation. Mutation of a single tryptophan to phenylalanine retunes the photoreceptor to detect UV-C wavelengths. Our analyses establish how UVR8 functions as a photoreceptor without a prosthetic chromophore to promote plant development and survival in sunlight.

PubMed: 22323738
DOI: 10.1126/science.1218091

実験手法

X-RAY DIFFRACTION (1.701 Å)