6lz7
From Proteopedia
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<StructureSection load='6lz7' size='340' side='right'caption='[[6lz7]], [[Resolution|resolution]] 3.60Å' scene=''> | <StructureSection load='6lz7' size='340' side='right'caption='[[6lz7]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LZ7 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5993617Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6lz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lz7 OCA], [https://pdbe.org/6lz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lz7 RCSB], [https://www.ebi.ac.uk/pdbsum/6lz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lz7 ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Cryptochrome 3D structures|Cryptochrome 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Shao K]] | |
| - | [[Category: Shao | + | [[Category: Zhang P]] |
| - | [[Category: Zhang | + | [[Category: Zhang X]] |
| - | [[Category: Zhang | + | |
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Current revision
Tetrameric structure of ZmCRY1a PHR domain
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