5XJX

Pre-formed plant receptor ERL1-TMM complex

Summary for 5XJX

• Entry DOI: 10.2210/pdb5xjx/pdb
• Descriptor: Protein TOO MANY MOUTHS, LRR receptor-like serine/threonine-protein kinase ERL1 (2 entities in total)
• Functional Keywords: receptor like kinase, receptor like protein, pre-formed complexe, transferase-membrane protein complex, transferase/membrane protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 12
• Total formula weight: 647895.80

Authors

Chai, J.,Lin, G.,Zhang, L.,Han, Z.,Yang, X.,Liu, W.,Qi, Y.,Chang, J.,Li, E. (deposition date: 2017-05-04, release date: 2019-01-23, Last modification date: 2023-11-22)

Primary citation

Lin, G.,Zhang, L.,Han, Z.,Yang, X.,Liu, W.,Li, E.,Chang, J.,Qi, Y.,Shpak, E.D.,Chai, J.
A receptor-like protein acts as a specificity switch for the regulation of stomatal development.
Genes Dev., 31:927-938, 2017

PubMed Abstract: Stomata are microscopic openings that allow for the exchange of gases between plants and the environment. In , stomatal patterning is specified by the ERECTA family (ERf) receptor kinases (RKs), the receptor-like protein (RLP) TOO MANY MOUTHS (TMM), and EPIDERMAL PATTERNING FACTOR (EPF) peptides. Here we show that TMM and ER or ER-LIKE1 (ERL1) form constitutive complexes, which recognize EPF1 and EPF2, but the single ERfs do not. TMM interaction with ERL1 creates a binding pocket for recognition of EPF1 and EPF2, indicating that the constitutive TMM-ERf complexes function as the receptors of EPF1 and EPF2. EPFL9 competes with EPF1 and EPF2 for binding to the ERf-TMM complex. EPFL4 and EPFL6, however, are recognized by the single ERfs without the requirement of TMM. In contrast to EPF1,2, the interaction of EPFL4,6 with an ERf is greatly reduced in the presence of TMM. Taken together, our data demonstrate that TMM dictates the specificity of ERfs for the perception of different EPFs, thus functioning as a specificity switch for the regulation of the activities of ERfs.

PubMed: 28536146
DOI: 10.1101/gad.297580.117

Experimental method

X-RAY DIFFRACTION (3.055 Å)