5luv
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Short LOV protein W619_1 in apo-state== | |
| + | <StructureSection load='5luv' size='340' side='right'caption='[[5luv]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5luv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_W619 Pseudomonas putida W619]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LUV 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]] 2.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5luv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5luv OCA], [https://pdbe.org/5luv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5luv RCSB], [https://www.ebi.ac.uk/pdbsum/5luv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5luv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B1J385_PSEPW B1J385_PSEPW] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Unique features of Light-Oxygen-Voltage (LOV) proteins like relatively small size (~12-19 kDa), inherent modularity, highly-tunable photocycle and oxygen-independent fluorescence have lately been exploited for the generation of optical tools. Structures of LOV domains reported so far contain a flavin chromophore per protein molecule. Here we report two new findings on the short LOV protein W619_1-LOV from Pseudomonas putida. First, the apo-state crystal structure of W619_1-LOV at 2.5 A resolution reveals conformational rearrangements in the secondary structure elements lining the chromophore pocket including elongation of the Falpha helix, shortening of the Ealpha-Falpha loop and partial unfolding of the Ealpha helix. Second, the apo W619_1-LOV protein binds both natural and structurally modified flavin chromophores. Remarkably different photophysical and photochemical properties of W619_1-LOV bound to 7-methyl-8-chloro-riboflavin (8-Cl-RF) and lumichrome imply application of these variants as novel optical tools as they offer advantages such as no adduct state formation, and a broader choice of wavelengths for in vitro studies. | ||
| - | + | Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools.,Arinkin V, Granzin J, Rollen K, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R Sci Rep. 2017 Feb 17;7:42971. doi: 10.1038/srep42971. PMID:28211532<ref>PMID:28211532</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5luv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas putida W619]] | ||
| + | [[Category: Arinkin V]] | ||
| + | [[Category: Batra-Safferling R]] | ||
| + | [[Category: Granzin J]] | ||
Current revision
Short LOV protein W619_1 in apo-state
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