5Y96
Crystal structure of ANXUR1 extracellular domain from Arabidopsis thaliana
Summary for 5Y96
| Entry DOI | 10.2210/pdb5y96/pdb |
| Related | 5Y92 |
| Descriptor | Receptor-like protein kinase ANXUR1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | receptor-like kinase, transferase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
| Cellular location | Cell membrane ; Single-pass type I membrane protein : Q9SR05 Q9SR05 |
| Total number of polymer chains | 2 |
| Total formula weight | 87498.61 |
| Authors | Du, S.,Xiao, J.Y. (deposition date: 2017-08-22, release date: 2018-02-28, Last modification date: 2024-11-06) |
| 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 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: 29388293DOI: 10.1002/pro.3381 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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