7BRC

Crystal structure of the TMK3 LRR domain

Summary for 7BRC

• Entry DOI: 10.2210/pdb7brc/pdb
• Descriptor: Receptor-like kinase TMK3, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: lrr, rlk, tmk, extracellular domain, plant protein, transferase
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 50271.23

Authors

Chen, H.,Kong, Y.Q.,Chen, J.,Li, L.,Li, X.S.,Yu, F.,Ming, Z.H. (deposition date: 2020-03-27, release date: 2020-08-19, Last modification date: 2024-10-30)

Primary citation

Chen, H.,Kong, Y.,Chen, J.,Li, L.,Li, X.,Yu, F.,Ming, Z.
Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from Arabidopsis thaliana.
Acta Crystallogr.,Sect.F, 76:384-390, 2020

PubMed Abstract: Transmembrane kinases (TMKs) are members of the plant receptor-like kinase (RLK) family. TMKs are characterized by an extracellular leucine-rich-repeat (LRR) domain, a single transmembrane region and a cytoplasmic kinase domain. TMKs have been shown to act as critical modulators of cell expansion and cell proliferation. Here, the crystal structure of the extracellular domain of TMK3 (TMK3-ECD) was determined to a resolution of 2.06 Å, with an R of 17.69% and an R of 20.58%. Similar to the extracellular domain of TMK1, the TMK3-ECD structure contains two solenoids with 13 LRRs and a non-LRR region (316-364) between the tenth and 11th LRRs. A comparison of TMK3-ECD with other LRR-RLKs that contain a non-LRR region indicates that the non-LRR region plays a critical role in structural integrity and may contribute to ligand interactions. The non-LRR region of TMK3-ECD is characterized by two disulfide bonds that may have critical biological implications.

PubMed: 32744250
DOI: 10.1107/S2053230X20010122

Experimental method

X-RAY DIFFRACTION (2.06 Å)