5GIJ

Crystal structure of TDR-TDIF complex

Summary for 5GIJ

• Entry DOI: 10.2210/pdb5gij/pdb
• Descriptor: Leucine-rich repeat receptor-like protein kinase TDR, Peptide from CLAVATA3/ESR (CLE)-related protein 41, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: lrr, tdr, tdif, pxy, lrr-rk, signaling protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 2
• Total formula weight: 72828.00

Authors

Morita, J.,Kato, K.,Ishitani, R.,Nishimasu, H.,Nureki, O. (deposition date: 2016-06-23, release date: 2016-08-24, Last modification date: 2023-11-08)

Primary citation

Morita, J.,Kato, K.,Nakane, T.,Kondo, Y.,Fukuda, H.,Nishimasu, H.,Ishitani, R.,Nureki, O.
Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide
Nat Commun, 7:12383-12383, 2016

PubMed Abstract: In plants, leucine-rich repeat receptor-like kinases (LRR-RKs) perceive ligands, including peptides and small molecules, to regulate various physiological processes. TDIF, a member of the CLE peptide family, specifically interacts with the LRR-RK TDR to inhibit meristem differentiation into tracheary elements, and promotes cell proliferation. Here we report the crystal structure of the extracellular domain of TDR in complex with the TDIF peptide. The extracellular domain of TDR adopts a superhelical structure comprising 22 LRRs, and specifically recognizes TDIF by its inner concave surface. Together with our biochemical and sequence analyses, our structure reveals a conserved TDIF-recognition mechanism of TDR among plant species. Furthermore, a structural comparison of TDR with other plant LRR-RKs suggested the activation mechanism of TDR by TDIF. The structure of this CLE peptide receptor provides insights into the recognition mechanism of the CLE family peptides.

PubMed: 27498761
DOI: 10.1038/ncomms12383

Experimental method

X-RAY DIFFRACTION (3 Å)