1UGL

Solution structure of S8-SP11

Summary for 1UGL

• Entry DOI: 10.2210/pdb1ugl/pdb
• NMR Information: BMRB: 5848
• Descriptor: S-locus pollen protein (1 entity in total)
• Functional Keywords: male determinant of self-incompatibility, defensin-like, sp11, scr, cysteine-rich, riken structural genomics/proteomics initiative, rsgi, structural genomics, plant protein
• Total number of polymer chains: 1
• Total formula weight: 5736.76

Authors

Mishima, M.,Takayama, S.,Sasaki, K.,Jee, J.G.,Kojima, C.,Isogai, A.,Shirakawa, M.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-06-16, release date: 2003-09-30, Last modification date: 2024-10-30)

Primary citation

Mishima, M.,Takayama, S.,Sasaki, K.,Jee, J.G.,Kojima, C.,Isogai, A.,Shirakawa, M.
Structure of the Male Determinant Factor for Brassica Self-incompatibility
J.Biol.Chem., 278:36389-36395, 2003

PubMed Abstract: Many flowering plants possess a self-incompatibility system to prevent inbreeding. In Brassica rapa, self/non-self recognition in mating is established through S-haplotype-specific interactions between stigma receptors and S-locus protein 11 (SP11, also called S-locus cysteine-rich protein) that is encoded at the highly polymorphic S-locus. Here we describe the solution structure of the SP11 protein of the S8-haplotype (S8-SP11), which specifically binds to the stigma factor of the same haplotype. It folds into an alpha/beta sandwich structure that resembles those of plant defensins. Residues important for structural integrity are highly conserved among the allelic SP11s, suggesting the existence of a common folding pattern. Structure-based sequence alignment and homology modeling of allelic SP11 identified a hyper-variable (HV) region, which is thought to form a loop that bulges out from the body of the protein that is amenable to solvent exposure. We suggest that the HV region could serve as a specific binding site for the stigma receptor.

PubMed: 12835321
DOI: 10.1074/jbc.M305305200

Experimental method

SOLUTION NMR