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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/A0A0M3PN85_STRHE A0A0M3PN85_STRHE] | | [https://www.uniprot.org/uniprot/A0A0M3PN85_STRHE A0A0M3PN85_STRHE] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5dnv" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
