6lz7 | pdb_00006lz7

Tetrameric structure of ZmCRY1a PHR domain

spinqualitylabelsall models 6lz7, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lz7 is a 1 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5993617Å Ligands: FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1D6HB67_MAIZE Publication Abstract from PubMed Cryptochromes (CRYs) are a group of evolutionarily conserved flavoproteins found in many organisms. In plants, the well-studied CRY photoreceptor, activated by blue light, plays essential roles in plant growth and development. However, the mechanism of activation remains largely unknown. Here, we determined the oligomeric structures of the blue-light-perceiving PHR domain of Zea mays CRY1 and an Arabidopsis CRY2 constitutively active mutant. The structures form dimers and tetramers whose functional importance is examined in vitro and in vivo with Arabidopsis CRY2. Structure-based analysis suggests that blue light may be perceived by CRY to cause conformational changes, whose precise nature remains to be determined, leading to oligomerization that is essential for downstream signaling. This photoactivation mechanism may be widely used by plant CRYs. Our study reveals a molecular mechanism of plant CRY activation and also paves the way for design of CRY as a more efficient optical switch. The oligomeric structures of plant cryptochromes.,Shao K, Zhang X, Li X, Hao Y, Huang X, Ma M, Zhang M, Yu F, Liu H, Zhang P Nat Struct Mol Biol. 2020 May;27(5):480-488. doi: 10.1038/s41594-020-0420-x. Epub, 2020 May 11. PMID:32398825 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cryptochrome 3D structures

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