4eer: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4eer]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. 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=4EER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EER FirstGlance]. <br>
-</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></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]] 1.753&#8491;</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></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=4eer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eer OCA], [https://pdbe.org/4eer PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eer RCSB], [https://www.ebi.ac.uk/pdbsum/4eer PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eer ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://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>
+[https://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 ==
-Fluorescent proteins derived from Light, Oxygen or Voltage (LOV) domains offer advantages over Green Fluorescent Protein (GFP) from their small size and efficacy under anaerobic conditions. The flavoprotein iLOV was engineered from the blue-light receptor phototropin as a reporter of viral infection. To inform the molecular basis for the improved, photoreversible, fluorescent properties of iLOV, we employed directed evolution and determined five LOV crystallographic structures. Comparative structural analyses between iLOV and its progenitors reveal mutation-induced constraints in the environment of the flavin mononcleotide (FMN) chromophore: in iLOV, the methyl group of Thr 394 crowds the FMN isoalloxazine ring, Leu470 triggers side-chain flipping of Leu472, and the terminal FMN phosphate shows increased anchoring. We further engineered iLOV variants that are readily detectable in bacterial and mammalian cells, due to order-of-magnitude photostability increases. Structure determination of a resulting representative photostable iLOV (phiLOV) variant reveals additional constraints on the chromophore. Aromatic residues Tyr401 and Phe485 in phiLOV sandwich the FMN isoalloxazine ring from both sides, while Ser390 anchors the side chain of FMN-interacting Gln489 Our combined structural and mutational results reveal that constraining the FMN fluorophore yields improved photochemical properties for iLOV and its new photostable derivative. These findings provide a framework for structural fine-tuning of LOV-scaffold proteins to maximize their potential as oxygen-independent fluorescent reporters.
-Structural Tuning of the Fluorescent Protein iLOV for Improved Photostability.,Christie JM, Hitomi K, Arvai AS, Hartfield KA, Mettlen M, Pratt AJ, Tainer JA, Getzoff ED J Biol Chem. 2012 May 9. PMID:22573334<ref>PMID:22573334</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4eer" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>