Structure of the OsSERK2 leucine-rich repeat extracellular domain

Ryan McAndrew, Rory N. Pruitt, Shizuo G. Kamita, Jose Henrique Pereira, Dipali Majumdar, Bruce D. Hammock, Paul D. Adams, Pamela C. Ronald

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Somatic embryogenesis receptor kinases (SERKs) are leucine-rich repeat (LRR)-containing integral membrane receptors that are involved in the regulation of development and immune responses in plants. It has recently been shown that rice SERK2 (OsSERK2) is essential for XA21-mediated resistance to the pathogen Xanthomonas oryzae pv. oryzae. OsSERK2 is also required for the BRI1-mediated, FLS2-mediated and EFR-mediated responses to brassinosteroids, flagellin and elongation factor Tu (EF-Tu), respectively. Here, crystal structures of the LRR domains of OsSERK2 and a D128N OsSERK2 mutant, expressed as hagfish variable lymphocyte receptor (VLR) fusions, are reported. These structures suggest that the aspartate mutation does not generate any significant conformational change in the protein, but instead leads to an altered interaction with partner receptors.

Original languageEnglish (US)
Pages (from-to)3080-3086
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume70
Issue number11
DOIs
StatePublished - Nov 1 2014

Keywords

  • leucine-rich repeats
  • OsSERK2
  • SERKs

ASJC Scopus subject areas

  • Structural Biology

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    McAndrew, R., Pruitt, R. N., Kamita, S. G., Pereira, J. H., Majumdar, D., Hammock, B. D., Adams, P. D., & Ronald, P. C. (2014). Structure of the OsSERK2 leucine-rich repeat extracellular domain. Acta Crystallographica Section D: Biological Crystallography, 70(11), 3080-3086. https://doi.org/10.1107/S1399004714021178