5ZT3
Crystal structure of WA352 from Oryza sativa
Summary for 5ZT3
| Entry DOI | 10.2210/pdb5zt3/pdb |
| Descriptor | WA352 (2 entities in total) |
| Functional Keywords | cytoplasmic male sterility protein, plant protein |
| Biological source | Oryza sativa subsp. indica (Rice) |
| Total number of polymer chains | 1 |
| Total formula weight | 14887.68 |
| Authors | |
| Primary citation | Wang, X.,Guan, Z.,Gong, Z.,Yan, J.,Yang, G.,Liu, Y.G.,Yin, P. Crystal structure of WA352 provides insight into cytoplasmic male sterility in rice Biochem. Biophys. Res. Commun., 501:898-904, 2018 Cited by PubMed Abstract: Plant cytoplasmic male sterility (CMS) is an important phenomenon and is widely utilized in hybrid crop breeding. The Wild Abortive CMS (CMS-WA), a well-known CMS type, has been successfully applied in the commercial production of hybrid rice seeds for more than 40 years. The CMS-WA causal gene WA352 encodes a novel transmenbrane protein and the interacts with the mitochondrial copper chaperone COX11, triggering reactive oxygen species production and resulting in male sterility in CMS-WA lines. However, the structure of WA352 is currently unknown, and the structural mechanism whereby WA352 perturbs COX11 function to cause CMS remains largely unknown. Here, we report the crystal structure of the C-terminal functional domain of WA352 at 1.3 Å resolution. This functional domain, consisting of five α helices, is spindle-shaped with a length of 42 Å, and a diameter of 28 Å. Notably, the absence of any structural similarity to a known protein structure suggests that the WA352 functional domain is a novel fold. In addition, surface conservation analysis and structural modeling of the WA352-COX11 complex revealed details about the WA352-COX11 interaction. Further structural analysis suggested that the WA352-COX11 interaction blocks the copper ion transportation activity of COX11, which is essential for the assembly of cytochrome c oxidase, resulting in male sterility in CMS-WA lines. Our study paves the way toward structural determination of the WA352-COX11 complex and provides new insight into the mechanism of plant CMS. PubMed: 29775612DOI: 10.1016/j.bbrc.2018.05.079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.304 Å) |
Structure validation
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