6gpv: Difference between revisions
New page: '''Unreleased structure''' The entry 6gpv is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Crystal structure of blue-light irradiated miniSOG== | |||
<StructureSection load='6gpv' size='340' side='right' caption='[[6gpv]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6gpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GPV FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=LUM:LUMICHROME'>LUM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=F7Q:'>F7Q</scene>, <scene name='pdbligand=HOO:'>HOO</scene>, <scene name='pdbligand=NFK:N-FORMYLKYNURENINE'>NFK</scene>, <scene name='pdbligand=OHI:3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE'>OHI</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHOT2, CAV1, KIN7, NPL1, At5g58140, K21L19.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=6gpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gpv OCA], [http://pdbe.org/6gpv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gpv RCSB], [http://www.ebi.ac.uk/pdbsum/6gpv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gpv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/PHOT2_ARATH PHOT2_ARATH]] Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Mediates calcium spiking of extra- and intracellular origins in response to blue light. Involved in hypocotyl phototropism. Contributes to the chloroplast accumulation in low blue light and mediates their translocation (avoidance response) at high fluence. Regulates stomata opening and photomorphogenesis response of leaf tissue. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening.<ref>PMID:11371609</ref> <ref>PMID:11251116</ref> <ref>PMID:12821778</ref> <ref>PMID:15031408</ref> <ref>PMID:14982991</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
miniSOG is the first flavin-binding protein that has been developed with the specific aim of serving as a genetically-encodable light-induced source of singlet oxygen ((1)O2). We have determined its 1.17 A resolution structure, which has allowed us to investigate its mechanism of photosensitization using an integrated approach combining spectroscopic and structural methods. Our results provide a structural framework to explain the ability of miniSOG to produce (1)O2 as a competition between oxygen- and protein quenching of its triplet state. In addition, a third excited-state decay pathway has been identified that is pivotal for the performance of miniSOG as (1)O2 photosensitizer, namely the photo-induced transformation of flavin mononucleotide (FMN) into lumichrome, which increases the accessibility of oxygen to the flavin FMN chromophore and makes protein quenching less favourable. The combination of the two effects explains the increase in the (1)O2 quantum yield by one order of magnitude upon exposure to blue light. Besides, we have identified several surface electron-rich residues that are progressively photo-oxidized, further contributing to facilitate the production of (1)O2. Our results help reconcile the apparent poor level of (1)O2 generation by miniSOG and its excellent performance in correlative light and electron microscopy experiments. | |||
Tailing miniSOG: structural bases of the complex photophysics of a flavin-binding singlet oxygen photosensitizing protein.,Torra J, Lafaye C, Signor L, Aumonier S, Flors C, Shu X, Nonell S, Gotthard G, Royant A Sci Rep. 2019 Feb 20;9(1):2428. doi: 10.1038/s41598-019-38955-3. PMID:30787421<ref>PMID:30787421</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6gpv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arath]] | |||
[[Category: Non-specific serine/threonine protein kinase]] | |||
[[Category: Aumonier, S]] | |||
[[Category: Gotthard, G]] | |||
[[Category: Lafaye, C]] | |||
[[Category: Royant, A]] | |||
[[Category: Shu, X]] | |||
[[Category: Signor, L]] | |||
[[Category: Flavoprotein]] | |||
[[Category: Fluorescent protein]] | |||
[[Category: Fmn]] | |||
[[Category: Gamma-peroxotyrosine]] | |||
[[Category: N-formylkynurenin]] | |||
[[Category: Oxidized histidine]] | |||
[[Category: Protein oxidation]] | |||
[[Category: Singlet oxygen]] | |||
Latest revision as of 11:23, 6 March 2019
Crystal structure of blue-light irradiated miniSOGCrystal structure of blue-light irradiated miniSOG
Structural highlights
Function[PHOT2_ARATH] Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Mediates calcium spiking of extra- and intracellular origins in response to blue light. Involved in hypocotyl phototropism. Contributes to the chloroplast accumulation in low blue light and mediates their translocation (avoidance response) at high fluence. Regulates stomata opening and photomorphogenesis response of leaf tissue. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening.[1] [2] [3] [4] [5] Publication Abstract from PubMedminiSOG is the first flavin-binding protein that has been developed with the specific aim of serving as a genetically-encodable light-induced source of singlet oxygen ((1)O2). We have determined its 1.17 A resolution structure, which has allowed us to investigate its mechanism of photosensitization using an integrated approach combining spectroscopic and structural methods. Our results provide a structural framework to explain the ability of miniSOG to produce (1)O2 as a competition between oxygen- and protein quenching of its triplet state. In addition, a third excited-state decay pathway has been identified that is pivotal for the performance of miniSOG as (1)O2 photosensitizer, namely the photo-induced transformation of flavin mononucleotide (FMN) into lumichrome, which increases the accessibility of oxygen to the flavin FMN chromophore and makes protein quenching less favourable. The combination of the two effects explains the increase in the (1)O2 quantum yield by one order of magnitude upon exposure to blue light. Besides, we have identified several surface electron-rich residues that are progressively photo-oxidized, further contributing to facilitate the production of (1)O2. Our results help reconcile the apparent poor level of (1)O2 generation by miniSOG and its excellent performance in correlative light and electron microscopy experiments. Tailing miniSOG: structural bases of the complex photophysics of a flavin-binding singlet oxygen photosensitizing protein.,Torra J, Lafaye C, Signor L, Aumonier S, Flors C, Shu X, Nonell S, Gotthard G, Royant A Sci Rep. 2019 Feb 20;9(1):2428. doi: 10.1038/s41598-019-38955-3. PMID:30787421[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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