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5Y92

Crystal structure of ANXUR2 extracellular domain from Arabidopsis thaliana

Summary for 5Y92
Entry DOI10.2210/pdb5y92/pdb
DescriptorReceptor-like protein kinase ANXUR2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsreceptor-like kinases, transferase
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Cellular locationCell membrane ; Single-pass type I membrane protein : Q3E8W4
Total number of polymer chains1
Total formula weight44636.67
Authors
Du, S.,Xiao, J.Y. (deposition date: 2017-08-22, release date: 2018-02-28, Last modification date: 2024-10-30)
Primary citationDu, S.,Qu, L.J.,Xiao, J.
Crystal structures of the extracellular domains of the CrRLK1L receptor-like kinases ANXUR1 and ANXUR2
Protein Sci., 27:886-892, 2018
Cited by
PubMed Abstract: Catharanthus roseus Receptor-Like Kinase 1-like (CrRLK1L) proteins contain two tandem malectin-like modules in their extracellular domains (ECDs) and function in diverse signaling pathways in plants. Malectin is a carbohydrate-binding protein in animals and recognizes a number of diglucosides; however, it remains unclear how the two malectin-like domains in the CrRLK1L proteins sense the ligand molecule. In this study, we reveal the crystal structures of the ECDs of ANXUR1 and ANXUR2, two CrRLK1L members in Arabidopsis thaliana that have critical functions in controlling pollen tube rupture during the fertilization process. We show that the two malectin-like domains in these proteins pack together to form a rigid architecture. Unlike animal malectin, these malectin-like domains lack residues involved in binding to the diglucosides, suggesting that they have a distinct ligand-binding mechanism. A cleft is observed between the two malectin-like domains, which might function as a potential ligand-binding pocket.
PubMed: 29388293
DOI: 10.1002/pro.3381
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.004 Å)
Structure validation

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