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4EBY

Crystal structure of the ectodomain of a receptor like kinase

Summary for 4EBY
Entry DOI10.2210/pdb4eby/pdb
Related4EBZ
DescriptorChitin elicitor receptor kinase 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 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 Keywordspathogen-associated molecular patterns, pattern recognition receptors, chitin elicitor receptor kinase 1, lysm, lysine motif, chitin oligomer, transferase
Biological sourceArabidopsis thaliana (mouse-ear cress,thale-cress)
Total number of polymer chains1
Total formula weight25537.03
Authors
Chai, J.,Liu, T.,Han, Z.,She, J,Wang, J. (deposition date: 2012-03-25, release date: 2012-06-27, Last modification date: 2024-11-06)
Primary citationLiu, 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: 22654057
DOI: 10.1126/science.1218867
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

227933

數據於2024-11-27公開中

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