5Y92

Crystal structure of ANXUR2 extracellular domain from Arabidopsis thaliana

Summary for 5Y92

• Entry DOI: 10.2210/pdb5y92/pdb
• Descriptor: Receptor-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 Keywords: receptor-like kinases, transferase
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Cellular location: Cell membrane ; Single-pass type I membrane protein : Q3E8W4
• Total number of polymer chains: 1
• Total formula weight: 44636.67

Authors

Du, S.,Xiao, J.Y. (deposition date: 2017-08-22, release date: 2018-02-28, Last modification date: 2024-10-30)

Primary citation

Du, 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

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

Experimental method

X-RAY DIFFRACTION (2.004 Å)