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Crystal structure of the LRR ectodomain of the plant immune receptor kinase SOBIR1

View ORCID ProfileUlrich Hohmann, View ORCID ProfileMichael Hothorn
doi: https://doi.org/10.1101/581231
Ulrich Hohmann
Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland
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Michael Hothorn
Structural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, 1211 Geneva, Switzerland
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Abstract

Plant unique membrane receptor kinases with leucine-rich repeat (LRR) extracellular domains are key regulators of development and immune responses. Here we present the 1.55 Å resolution crystal structure of the immune receptor kinase SOBIR1 from Arabidopsis. The ectodomain structure reveals the presence of 5 LRRs sandwiched between non-canonical capping domains. The disulphide bond-stabilized N-terminal cap harbors an unusual β-hairpin structure. The C-terminal cap features a highly positively charged linear motif which we find largely disordered in our structure. Size-exclusion chromatography and right-angle light scattering experiments suggest that SOBIR1 is a monomer in solution. The protruding β-hairpin, a set of highly conserved basic residues at the inner surface of the SOBIR LRR domain and the presence of a genetic missense allele in LRR2, together suggest that the SOBIR1 ectodomain may mediate protein – protein interaction in plant immune signalling.

Synopsis The ectodomain structure of a novel plant membrane receptor kinase with unusual capping domains is reported.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted March 18, 2019.
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Crystal structure of the LRR ectodomain of the plant immune receptor kinase SOBIR1
Ulrich Hohmann, Michael Hothorn
bioRxiv 581231; doi: https://doi.org/10.1101/581231
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Crystal structure of the LRR ectodomain of the plant immune receptor kinase SOBIR1
Ulrich Hohmann, Michael Hothorn
bioRxiv 581231; doi: https://doi.org/10.1101/581231

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