5dnu
From Proteopedia
Crystal structure of Striga KAI2-like protein in complex with karrikin
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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