4fof: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4fof]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FOF FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=VRB:PHYCOVIOLOBILIN,+BLUE+LIGHT-ABSORBING+FORM'>VRB</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.416&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=VRB:PHYCOVIOLOBILIN,+BLUE+LIGHT-ABSORBING+FORM'>VRB</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=4fof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fof OCA], [https://pdbe.org/4fof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fof RCSB], [https://www.ebi.ac.uk/pdbsum/4fof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fof ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/Q8DLC7_THEVB Q8DLC7_THEVB]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The phytochrome superfamily encompasses a diverse collection of photochromic photoreceptors in plants and microorganisms that employ a covalently linked bilin cradled in a cGMP-phosphodiesterase/adenylyl-cyclase/FhlA (GAF) domain to detect light. Whereas most interconvert between red- and far-red-light-absorbing states, cyanobacteria also express variants called cyanobacteriochromes (CBCRs) that modify bilin absorption to collectively perceive the entire visible spectrum. Here, we present two X-ray crystallographic structures of the GAF domain from the blue/green photochromic CBCR PixJ from Thermosynechococcus elongatus. These structures confirm the hypothesis that CBCRs variably manipulate the chromophore pi-conjugation system through isomerization and a second thioether linkage, in this case involving the bilin C10 carbon and Cys494 within a DXCF sequence characteristic of blue/green CBCRs. Biochemical studies support a mechanism for photoconversion whereby the second linkage ruptures on route to the green-light-absorbing state. Collectively, the TePixJ(GAF) models illustrate the remarkable structural and photochemical versatility among phytochromes and CBCRs in driving light perception.
-A Photo-Labile Thioether Linkage to Phycoviolobilin Provides the Foundation for the Blue/Green Photocycles in DXCF-Cyanobacteriochromes.,Burgie ES, Walker JM, Phillips GN Jr, Vierstra RD Structure. 2013 Jan 8;21(1):88-97. doi: 10.1016/j.str.2012.11.001. Epub 2012 Dec , 6. PMID:23219880<ref>PMID:23219880</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4fof" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>