View source for 5cbk


==Crystal structure of the strigolactone receptor ShHTL5 from Striga hermonthica==
<StructureSection load='5cbk' size='340' side='right'caption='[[5cbk]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cbk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Striga_hermonthica Striga hermonthica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CBK 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]] 2.462&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PE3:3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL'>PE3</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=5cbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cbk OCA], [https://pdbe.org/5cbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cbk RCSB], [https://www.ebi.ac.uk/pdbsum/5cbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cbk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M5I297_STRHE A0A0M5I297_STRHE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Strigolactones are naturally occurring signaling molecules that affect plant development, fungi-plant interactions, and parasitic plant infestations. We characterized the function of 11 strigolactone receptors from the parasitic plant Striga hermonthica using chemical and structural biology. We found a clade of polyspecific receptors, including one that is sensitive to picomolar concentrations of strigolactone. A crystal structure of a highly sensitive strigolactone receptor from Striga revealed a larger binding pocket than that of the Arabidopsis receptor, which could explain the increased range of strigolactone sensitivity. Thus, the sensitivity of Striga to strigolactones from host plants is driven by receptor sensitivity. By expressing strigolactone receptors in Arabidopsis, we developed a bioassay that can be used to identify chemicals and crops with altered strigolactone levels.

Structure-function analysis identifies highly sensitive strigolactone receptors in Striga.,Toh S, Holbrook-Smith D, Stogios PJ, Onopriyenko O, Lumba S, Tsuchiya Y, Savchenko A, McCourt P Science. 2015 Oct 9;350(6257):203-7. doi: 10.1126/science.aac9476. PMID:26450211<ref>PMID:26450211</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cbk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Striga hermonthica]]
[[Category: Onopriyenko O]]
[[Category: Savchenko A]]
[[Category: Stogios PJ]]
[[Category: Yim V]]