6KYW
S8-mSRK-S8-SP11 complex
Summary for 6KYW
| Entry DOI | 10.2210/pdb6kyw/pdb |
| Descriptor | Receptor protein kinase SRK8, S locus protein 11, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | ligand-receptor complex, plant protein |
| Biological source | Brassica campestris (Field mustard) More |
| Total number of polymer chains | 4 |
| Total formula weight | 112623.22 |
| Authors | Murase, K.,Hakoshima, T.,Mori, T. (deposition date: 2019-09-20, release date: 2020-09-16, Last modification date: 2024-11-20) |
| Primary citation | Murase, K.,Moriwaki, Y.,Mori, T.,Liu, X.,Masaka, C.,Takada, Y.,Maesaki, R.,Mishima, M.,Fujii, S.,Hirano, Y.,Kawabe, Z.,Nagata, K.,Terada, T.,Suzuki, G.,Watanabe, M.,Shimizu, K.,Hakoshima, T.,Takayama, S. Mechanism of self/nonself-discrimination in Brassica self-incompatibility. Nat Commun, 11:4916-4916, 2020 Cited by PubMed Abstract: Self-incompatibility (SI) is a breeding system that promotes cross-fertilization. In Brassica, pollen rejection is induced by a haplotype-specific interaction between pistil determinant SRK (S receptor kinase) and pollen determinant SP11 (S-locus Protein 11, also named SCR) from the S-locus. Although the structure of the B. rapa S-SRK ectodomain (eSRK) and S-SP11 complex has been determined, it remains unclear how SRK discriminates self- and nonself-SP11. Here, we uncover the detailed mechanism of self/nonself-discrimination in Brassica SI by determining the S-eSRK-S-SP11 crystal structure and performing molecular dynamics (MD) simulations. Comprehensive binding analysis of eSRK and SP11 structures reveals that the binding free energies are most stable for cognate eSRK-SP11 combinations. Residue-based contribution analysis suggests that the modes of eSRK-SP11 interactions differ between intra- and inter-subgroup (a group of phylogenetically neighboring haplotypes) combinations. Our data establish a model of self/nonself-discrimination in Brassica SI. PubMed: 33004803DOI: 10.1038/s41467-020-18698-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.60112735603 Å) |
Structure validation
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