View source for 5dnu


==Crystal structure of Striga KAI2-like protein in complex with karrikin==
<StructureSection load='5dnu' size='340' side='right'caption='[[5dnu]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dnu]] 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=5DNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DNU 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]] 1.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KKN:3-METHYL-2H-FURO[2,3-C]PYRAN-2-ONE'>KKN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5dnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dnu OCA], [https://pdbe.org/5dnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dnu RCSB], [https://www.ebi.ac.uk/pdbsum/5dnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dnu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M3PN85_STRHE A0A0M3PN85_STRHE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The perception of two plant germination inducers, karrikins and strigolactones, are mediated by the proteins KAI2 and D14. Recently, KAI2-type proteins from parasitic weeds, which are possibly related to seed germination induced by strigolactone, have been classified into three clades characterized by different responses to karrikin/strigolactone. Here we characterized a karrikin-binding protein in Striga (ShKAI2iB) that belongs to intermediate-evolving KAI2 and provided the structural bases for its karrikin-binding specificity. Binding assays showed that ShKAI2iB bound karrikins but not strigolactone, differing from other KAI2 and D14. The crystal structures of ShKAI2iB and ShKAI2iB-karrikin complex revealed obvious structural differences in a helix located at the entry of its ligand-binding cavity. This results in a smaller closed pocket, which is also the major cause of ShKAI2iB's specificity of binding karrikin. Our structural study also revealed that a few non-conserved amino acids led to the distinct ligand-binding profile of ShKAI2iB, suggesting that the evolution of KAI2 resulted in its diverse functions.

Structural basis of unique ligand specificity of KAI2-like protein from parasitic weed Striga hermonthica.,Xu Y, Miyakawa T, Nakamura H, Nakamura A, Imamura Y, Asami T, Tanokura M Sci Rep. 2016 Aug 10;6:31386. doi: 10.1038/srep31386. PMID:27507097<ref>PMID:27507097</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dnu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Striga hermonthica]]
[[Category: Miyakawa T]]
[[Category: Nakamura A]]
[[Category: Tanokura M]]
[[Category: Xu Y]]