This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5luv
From Proteopedia
(Difference between revisions)
m (Protected "5luv" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LUV 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=SO4:SULFATE+ION'>SO4</scene></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=5luv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5luv OCA], [http://pdbe.org/5luv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5luv RCSB], [http://www.ebi.ac.uk/pdbsum/5luv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5luv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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: Arinkin, V]] | ||
| + | [[Category: Batra-Safferling, R]] | ||
| + | [[Category: Granzin, J]] | ||
| + | [[Category: Apo-state]] | ||
| + | [[Category: Lov domain]] | ||
| + | [[Category: Pas domain]] | ||
| + | [[Category: Signaling protein]] | ||
Revision as of 07:39, 9 March 2017
Short LOV protein W619_1 in apo-state
| |||||||||||
