4EBZ
Crystal structure of the ectodomain of a receptor like kinase
Summary for 4EBZ
Entry DOI | 10.2210/pdb4ebz/pdb |
Related | 4EBY |
Descriptor | Chitin elicitor receptor kinase 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | pathogen-associated molecular patterns, pattern recognition receptors, chitin elicitor receptor kinase 1, lysm, lysine motif, chitin oligomer, transferase |
Biological source | Arabidopsis thaliana (mouse-ear cress) |
Total number of polymer chains | 1 |
Total formula weight | 26470.89 |
Authors | |
Primary citation | Liu, T.,Liu, Z.,Song, C.,Hu, Y.,Han, Z.,She, J.,Fan, F.,Wang, J.,Jin, C.,Chang, J.,Zhou, J.M.,Chai, J. Chitin-induced dimerization activates a plant immune receptor. Science, 336:1160-1164, 2012 Cited by PubMed Abstract: Pattern recognition receptors confer plant resistance to pathogen infection by recognizing the conserved pathogen-associated molecular patterns. The cell surface receptor chitin elicitor receptor kinase 1 of Arabidopsis (AtCERK1) directly binds chitin through its lysine motif (LysM)-containing ectodomain (AtCERK1-ECD) to activate immune responses. The crystal structure that we solved of an AtCERK1-ECD complexed with a chitin pentamer reveals that their interaction is primarily mediated by a LysM and three chitin residues. By acting as a bivalent ligand, a chitin octamer induces AtCERK1-ECD dimerization that is inhibited by shorter chitin oligomers. A mutation attenuating chitin-induced AtCERK1-ECD dimerization or formation of nonproductive AtCERK1 dimer by overexpression of AtCERK1-ECD compromises AtCERK1-mediated signaling in plant cells. Together, our data support the notion that chitin-induced AtCERK1 dimerization is critical for its activation. PubMed: 22654057DOI: 10.1126/science.1218867 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.792 Å) |
Structure validation
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