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| | ==Crystal Structure of Rhodobacter Sphaeroides LOV protein== | | ==Crystal Structure of Rhodobacter Sphaeroides LOV protein== |
| - | <StructureSection load='4hnb' size='340' side='right' caption='[[4hnb]], [[Resolution|resolution]] 2.34Å' scene=''> | + | <StructureSection load='4hnb' size='340' side='right'caption='[[4hnb]], [[Resolution|resolution]] 2.34Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hnb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhos5 Rhos5]. The March 2015 RCSB PDB [http://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 [http://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=4HNB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HNB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hnb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides_ATCC_17025 Cereibacter sphaeroides ATCC 17025]. 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=4HNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HNB 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>, <scene name='pdbligand=FNR:1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL'>FNR</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=FNR:1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL'>FNR</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hj4|4hj4]], [[4hj6|4hj6]], [[4hia|4hia]], [[4hj3|4hj3]]</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=4hnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hnb OCA], [https://pdbe.org/4hnb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hnb RCSB], [https://www.ebi.ac.uk/pdbsum/4hnb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hnb ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rhodobacter sphaeroides ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=349102 RHOS5])</td></tr>
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| - | <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=4hnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hnb OCA], [http://pdbe.org/4hnb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hnb RCSB], [http://www.ebi.ac.uk/pdbsum/4hnb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hnb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/M1E1F8_CERS5 M1E1F8_CERS5] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Cereibacter sphaeroides ATCC 17025]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Phototropin]] | | [[Category: Phototropin]] |
| | [[Category: RCSB PDB Molecule of the Month]] | | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Rhos5]]
| + | [[Category: Bilwes AM]] |
| - | [[Category: Bilwes, A M]] | + | [[Category: Conrad KS]] |
| - | [[Category: Conrad, K S]] | + | [[Category: Crane BR]] |
| - | [[Category: Crane, B R]] | + | |
| - | [[Category: Lov pas hth]]
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| - | [[Category: Signaling]]
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| - | [[Category: Signaling protein]]
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| Structural highlights
Function
M1E1F8_CERS5
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Conrad KS, Bilwes AM, Crane BR. Light-Induced Subunit Dissociation by a Light-Oxygen-Voltage Domain Photoreceptor from Rhodobacter sphaeroides. Biochemistry. 2013 Jan 15;52(2):378-91. doi: 10.1021/bi3015373. Epub 2013 Jan 3. PMID:23252338 doi:10.1021/bi3015373
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