View source for 4wf0


==Crystal Structure of iLID - an Improved Light-Inducible Dimer==
<StructureSection load='4wf0' size='340' side='right'caption='[[4wf0]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wf0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Avena_sativa Avena sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WF0 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]] 1.95&#8491;</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=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=4wf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wf0 OCA], [https://pdbe.org/4wf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wf0 RCSB], [https://www.ebi.ac.uk/pdbsum/4wf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wf0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O49003_AVESA O49003_AVESA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The discovery of light-inducible protein-protein interactions has allowed for the spatial and temporal control of a variety of biological processes. To be effective, a photodimerizer should have several characteristics: it should show a large change in binding affinity upon light stimulation, it should not cross-react with other molecules in the cell, and it should be easily used in a variety of organisms to recruit proteins of interest to each other. To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa. In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB. Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation. Here, we describe the use of computational protein design, phage display, and high-throughput binding assays to create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation. A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark. We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.

Engineering an improved light-induced dimer (iLID) for controlling the localization and activity of signaling proteins.,Guntas G, Hallett RA, Zimmerman SP, Williams T, Yumerefendi H, Bear JE, Kuhlman B Proc Natl Acad Sci U S A. 2014 Dec 22. pii: 201417910. PMID:25535392<ref>PMID:25535392</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wf0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Avena sativa]]
[[Category: Large Structures]]
[[Category: Hallett R]]
[[Category: Kuhlman B]]
[[Category: Williams T]]