3rh8: Difference between revisions
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==Crystal Structure of the Light-state Dimer of Fungal Blue-Light Photoreceptor Vivid== | |||
<StructureSection load='3rh8' size='340' side='right'caption='[[3rh8]], [[Resolution|resolution]] 2.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3rh8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. The March 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phototropin'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_3 10.2210/rcsb_pdb/mom_2015_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RH8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> | |||
<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'>[https://proteopedia.org/fgij/fg.htm?mol=3rh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rh8 OCA], [https://pdbe.org/3rh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rh8 RCSB], [https://www.ebi.ac.uk/pdbsum/3rh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rh8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9C3Y6_NEUCS Q9C3Y6_NEUCS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Light, oxygen, or voltage (LOV) protein domains are present in many signaling proteins in bacteria, archaea, protists, plants, and fungi. The LOV protein VIVID (VVD) of the filamentous fungus Neurospora crassa enables the organism to adapt to constant or increasing amounts of light and facilitates proper entrainment of circadian rhythms. Here, we determined the crystal structure of the fully light-adapted VVD dimer and reveal the mechanism by which light-driven conformational change alters the oligomeric state of the protein. Light-induced formation of a cysteinyl-flavin adduct generated a new hydrogen bond network that released the amino (N) terminus from the protein core and restructured an acceptor pocket for binding of the N terminus on the opposite subunit of the dimer. Substitution of residues critical for the switch between the monomeric and the dimeric states of the protein had profound effects on light adaptation in Neurospora. The mechanism of dimerization of VVD provides molecular details that explain how members of a large family of photoreceptors convert light responses to alterations in protein-protein interactions. | |||
Structure of a Light-Activated LOV Protein Dimer That Regulates Transcription.,Vaidya AT, Chen CH, Dunlap JC, Loros JJ, Crane BR Sci Signal. 2011 Aug 2;4(184):ra50. PMID:21868352<ref>PMID:21868352</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3rh8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neurospora crassa]] | |||
[[Category: Phototropin]] | |||
[[Category: RCSB PDB Molecule of the Month]] | |||
[[Category: Crane BR]] | |||
[[Category: Vaidya AT]] | |||
Latest revision as of 05:21, 21 November 2024
Crystal Structure of the Light-state Dimer of Fungal Blue-Light Photoreceptor VividCrystal Structure of the Light-state Dimer of Fungal Blue-Light Photoreceptor Vivid
Structural highlights
FunctionPublication Abstract from PubMedLight, oxygen, or voltage (LOV) protein domains are present in many signaling proteins in bacteria, archaea, protists, plants, and fungi. The LOV protein VIVID (VVD) of the filamentous fungus Neurospora crassa enables the organism to adapt to constant or increasing amounts of light and facilitates proper entrainment of circadian rhythms. Here, we determined the crystal structure of the fully light-adapted VVD dimer and reveal the mechanism by which light-driven conformational change alters the oligomeric state of the protein. Light-induced formation of a cysteinyl-flavin adduct generated a new hydrogen bond network that released the amino (N) terminus from the protein core and restructured an acceptor pocket for binding of the N terminus on the opposite subunit of the dimer. Substitution of residues critical for the switch between the monomeric and the dimeric states of the protein had profound effects on light adaptation in Neurospora. The mechanism of dimerization of VVD provides molecular details that explain how members of a large family of photoreceptors convert light responses to alterations in protein-protein interactions. Structure of a Light-Activated LOV Protein Dimer That Regulates Transcription.,Vaidya AT, Chen CH, Dunlap JC, Loros JJ, Crane BR Sci Signal. 2011 Aug 2;4(184):ra50. PMID:21868352[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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