5GQR
Crystal structure of PXY-CLE41-SERK2
Summary for 5GQR
Entry DOI | 10.2210/pdb5gqr/pdb |
Descriptor | Leucine-rich repeat receptor-like protein kinase TDR, TDIF, Somatic embryogenesis receptor kinase 2, ... (4 entities in total) |
Functional Keywords | meristem cell proliferation, serk, cle peptides, leucine rich repeat, transferase |
Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
Total number of polymer chains | 3 |
Total formula weight | 88194.26 |
Authors | Chai, J.J.,Zhang, H.Q. (deposition date: 2016-08-08, release date: 2016-12-14, Last modification date: 2023-11-08) |
Primary citation | Zhang, H.Q.,Lin, X.Y.,Han, Z.F.,Wang, J.,Qu, L.J.,Chai, J.J. SERK Family Receptor-like Kinases Function as Co-receptors with PXY for Plant Vascular Development Mol Plant, 9:1406-1414, 2016 Cited by PubMed Abstract: In Arabidopsis, the CLAVATA3/EMBRYO SURROUNDING REGION-RELATED (CLE) peptides play important roles in regulating proliferation and differentiation of plant-specific stem cells. Although receptors of CLEs are reported to be leucine-rich repeat receptor kinases, the mechanisms underlying CLE-induced receptor activation remain largely unknown. Here we show that SOMATIC EMBRYOGENESIS RECEPTOR KINASEs (SERKs) serve as co-receptors in CLE41/TDIF-PXY signaling to regulate plant vascular development. TDIF induces interaction of its receptor PXY with SERKs in vitro and in vivo. Furthermore, the serk1-1 serk2-1 bak1-5 mutant plants are less sensitive to TDIF, phenocopying the pxy mutant with a compromised promotion of procambial cell proliferation. Crystal structure of the PXY-TDIF-SERK2 complex reveals that the last amino acid of TDIF conserved among CLEs and other evolutionary-related peptides is important for the interaction between SERK2 and PXY. Taken together, our current study identifies SERKs as signaling components of the TDIF-PXY pathway and suggests a conserved activation mechanism of CLE receptors. PubMed: 27449136DOI: 10.1016/j.molp.2016.07.004 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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