4hj4: Difference between revisions
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==Crystal Structure of Rhodobacter Sphaeroides LOV protein== | |||
=== | <StructureSection load='4hj4' size='340' side='right' caption='[[4hj4]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hj4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides_atcc_17025 Rhodobacter sphaeroides atcc 17025]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HJ4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hia|4hia]], [[4hj3|4hj3]], [[4hj6|4hj6]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hj4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hj4 RCSB], [http://www.ebi.ac.uk/pdbsum/4hj4 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Light-oxygen-voltage (LOV) domains bind a flavin chromophore to serve as blue light sensors in a wide range of eukaryotic and prokaryotic proteins. LOV domains are associated with a variable effector domain or a separate protein signaling partner to execute a wide variety of functions that include regulation of kinases, generation of anti-sigma factor antagonists, and regulation of circadian clocks. Here we present the crystal structure, photocycle kinetics, association properties, and spectroscopic features of a full-length LOV domain protein from Rhodobacter sphaeroides (RsLOV). RsLOV exhibits N- and C-terminal helical extensions that form an unusual helical bundle at its dimer interface with some resemblance to the helical transducer of sensory rhodopsin II. The blue light-induced conformational changes of RsLOV revealed from a comparison of light- and dark-state crystal structures support a shared signaling mechanism of LOV domain proteins that originates with the light-induced formation of a flavin-cysteinyl photoadduct. Adduct formation disrupts hydrogen bonding in the active site and propagates structural changes through the LOV domain core to the N- and C-terminal extensions. Single-residue variants in the active site and dimer interface of RsLOV alter photoadduct lifetimes and induce structural changes that perturb the oligomeric state. Size exclusion chromatography, multiangle light scattering, small-angle X-ray scattering, and cross-linking studies indicate that RsLOV dimerizes in the dark but, upon light excitation, dissociates into monomers. This light-induced switch in oligomeric state may prove to be useful for engineering molecular associations in controlled cellular settings. | |||
Light-Induced Subunit Dissociation by a Light-Oxygen-Voltage Domain Photoreceptor from Rhodobacter sphaeroides.,Conrad KS, Bilwes AM, Crane BR Biochemistry. 2013 Jan 15;52(2):378-91. doi: 10.1021/bi3015373. Epub 2013 Jan 3. PMID:23252338<ref>PMID:23252338</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Rhodobacter sphaeroides atcc 17025]] | [[Category: Rhodobacter sphaeroides atcc 17025]] | ||
[[Category: Bilwes, A M | [[Category: Bilwes, A M]] | ||
[[Category: Conrad, K S | [[Category: Conrad, K S]] | ||
[[Category: Crane, B R | [[Category: Crane, B R]] | ||
[[Category: Hth]] | [[Category: Hth]] | ||
[[Category: Lov]] | [[Category: Lov]] | ||
[[Category: Pa]] | [[Category: Pa]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 16:09, 21 December 2014
Crystal Structure of Rhodobacter Sphaeroides LOV proteinCrystal Structure of Rhodobacter Sphaeroides LOV protein
Structural highlights
Publication Abstract from PubMedLight-oxygen-voltage (LOV) domains bind a flavin chromophore to serve as blue light sensors in a wide range of eukaryotic and prokaryotic proteins. LOV domains are associated with a variable effector domain or a separate protein signaling partner to execute a wide variety of functions that include regulation of kinases, generation of anti-sigma factor antagonists, and regulation of circadian clocks. Here we present the crystal structure, photocycle kinetics, association properties, and spectroscopic features of a full-length LOV domain protein from Rhodobacter sphaeroides (RsLOV). RsLOV exhibits N- and C-terminal helical extensions that form an unusual helical bundle at its dimer interface with some resemblance to the helical transducer of sensory rhodopsin II. The blue light-induced conformational changes of RsLOV revealed from a comparison of light- and dark-state crystal structures support a shared signaling mechanism of LOV domain proteins that originates with the light-induced formation of a flavin-cysteinyl photoadduct. Adduct formation disrupts hydrogen bonding in the active site and propagates structural changes through the LOV domain core to the N- and C-terminal extensions. Single-residue variants in the active site and dimer interface of RsLOV alter photoadduct lifetimes and induce structural changes that perturb the oligomeric state. Size exclusion chromatography, multiangle light scattering, small-angle X-ray scattering, and cross-linking studies indicate that RsLOV dimerizes in the dark but, upon light excitation, dissociates into monomers. This light-induced switch in oligomeric state may prove to be useful for engineering molecular associations in controlled cellular settings. Light-Induced Subunit Dissociation by a Light-Oxygen-Voltage Domain Photoreceptor from Rhodobacter sphaeroides.,Conrad KS, Bilwes AM, Crane BR Biochemistry. 2013 Jan 15;52(2):378-91. doi: 10.1021/bi3015373. Epub 2013 Jan 3. PMID:23252338[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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