View source for 7wa8


==Strigolactone receptors in Striga ShHTL7==
<StructureSection load='7wa8' size='340' side='right'caption='[[7wa8]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wa8]] is a 2 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=7WA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WA8 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]] 2.33&#8491;</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=7wa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wa8 OCA], [https://pdbe.org/7wa8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wa8 RCSB], [https://www.ebi.ac.uk/pdbsum/7wa8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wa8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M3PNA2_STRHE A0A0M3PNA2_STRHE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Seeds of the root parasitic plant Striga hermonthica can sense very low concentrations of strigolactones (SLs) exuded from host roots. The S. hermonthica hyposensitive to light (ShHTL) proteins are putative SL receptors, among which ShHTL7 reportedly confers sensitivity to picomolar levels of SL when expressed in Arabidopsis thaliana. However, the molecular mechanism underlying ShHTL7 sensitivity is unknown. Here we determined the ShHTL7 crystal structure and quantified its interactions with various SLs and key interacting proteins. We established that ShHTL7 has an active-site pocket with broad-spectrum response to different SLs and moderate affinity. However, in contrast to other ShHTLs, we observed particularly high affinity of ShHTL7 for F-box protein AtMAX2. Furthermore, ShHTL7 interacted with AtMAX2 and with transcriptional regulator AtSMAX1 in response to nanomolar SL concentration. ShHTL7 mutagenesis analyses identified surface residues that contribute to its high-affinity binding to AtMAX2 and residues in the ligand binding pocket that confer broad-spectrum response to SLs with various structures. Crucially, yeast-three hybrid experiments showed that AtMAX2 confers responsiveness of the ShHTL7-AtSMAX1 interaction to picomolar levels of SL in line with the previously reported physiological sensitivity. These findings highlight the key role of SL-induced MAX2-ShHTL7-SMAX1 complex formation in determining the sensitivity to SL. Moreover, these data suggest a strategy to screen for compounds that could promote suicidal seed germination at physiologically relevant levels.

Molecular basis for high ligand sensitivity and selectivity of strigolactone receptors in Striga.,Wang Y, Yao R, Du X, Guo L, Chen L, Xie D, Smith SM Plant Physiol. 2021 Apr 23;185(4):1411-1428. doi: 10.1093/plphys/kiaa048. PMID:33793945<ref>PMID:33793945</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wa8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Striga hermonthica]]
[[Category: Wang Y]]
[[Category: Yao R]]