6dd7

Crystal structure of plant UVB photoreceptor UVR8 from in situ serial Laue diffraction

spinqualitylabelsall models 6dd7, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6dd7 is a 4 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: UVR8, At5g63860, MGI19.7 (ARATH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [UVR8_ARATH] UV-B specific signaling component that acts as UV-B photoreceptor and plays a key role in establishing UV-protective responses in plants. Upon UV-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, accumulates in the nucleus, interacts with the photomorphogenic repressor COP1 and regulates the expression of the transcription factor HY5 by associating with chromatin (through histone H2B binding) in the HY5 promoter region. UVR8 is involved in controlling aspects of leaf growth and morphogenesis in response to UV-B, is required for normal progression of endocycle and has a regulatory role in stomatal differentiation. Is required for plant circadian clock response to photomorphogenic UV-B light, partly through the transcriptional activation of responsive clock genes. Promotes photosynthetic efficiency at elevated levels of UV-B. Plays a role in mediating the effects of UV-B radiation on pathogen resistance by controlling the expression of the sinapate biosynthetic pathway. The two tryptophans, Trp-285 and Trp-233, serve collectively as the UV-B chromophore. Publication Abstract from PubMed Recent developments in serial crystallography at X-ray free electron lasers (XFELs) and synchrotrons have been driven by two scientific goals in structural biology - first, static structure determination from nano or microcrystals of membrane proteins and large complexes that are difficult for conventional cryocrystallography, and second, direct observations of transient structural species in biochemical reactions at near atomic resolution. Since room-temperature diffraction experiments naturally demand a large quantity of purified protein, sample economy is critically important for all steps of serial crystallography from crystallization, crystal delivery to data collection. Here we report the development and applications of "crystal-on-crystal" devices to facilitate large-scale in situ serial diffraction experiments on protein crystals of all sizes - large, small, or microscopic. We show that the monocrystalline quartz as a substrate material prevents vapor loss during crystallization and significantly reduces background X-ray scattering. These devices can be readily adopted at XFEL and synchrotron beamlines, which enable efficient delivery of hundreds to millions of crystals to the X-ray beam, with an overall protein consumption per dataset comparable to that of cryocrystallography. Crystal-on-crystal chips for in situ serial diffraction at room temperature.,Ren Z, Ayhan M, Bandara S, Bowatte K, Kumarapperuma I, Gunawardana S, Shin H, Wang C, Zeng X, Yang X Lab Chip. 2018 Jun 28. doi: 10.1039/c8lc00489g. PMID:29952383 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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