5HXL
Structure based function annotation of a hypothetical protein MGG_01005 related to the development of rice blast fungus
Summary for 5HXL
Entry DOI | 10.2210/pdb5hxl/pdb |
Related | 5HYC |
Descriptor | dynein light chain Tctex-1 (2 entities in total) |
Functional Keywords | dynein light chain tctex-1, unknown function |
Biological source | Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) |
Total number of polymer chains | 1 |
Total formula weight | 16854.84 |
Authors | |
Primary citation | Li, G.,Huang, J.,Yang, J.,He, D.,Wang, C.,Qi, X.,Taylor, I.A.,Liu, J.,Peng, Y.L. Structure based function-annotation of hypothetical protein MGG_01005 from Magnaporthe oryzae reveals it is the dynein light chain orthologue of dynlt1/3. Sci Rep, 8:3952-3952, 2018 Cited by PubMed Abstract: Magnaporthe oryzae is a model fungal plant pathogen employed for studying plant-fungi interactions. Whole genome sequencing and bioinformatics analyses revealed that this fungal pathogen has more than 12,000 protein-coding genes with 65% of the genes remaining functionally un-annotated. Here, we determine the structure of the hypothetical protein, MGG_01005 and show that it is the Magnaporthe oryzae Dynein light chain Tctex-type 1 (dynlt1/3), demonstrated by its structural similarity to other orthologous dynlt1 proteins and its conserved interaction with the N-terminus of the Magnaporthe oryzae dynein intermediate chain, MoDyn1I2. In addition, we present the structure of the MGG_01005-MoDyn1I2 complex together with mutagenesis studies that reveals a di-histidine motif interaction with a glutamate residue in the dynein intermediate chain within a conserved molecular interface. These results demonstrate the utility of structure-based annotation and validate it as a viable approach for the molecular assignment of hypothetic proteins from phyto-pathogenic fungi. PubMed: 29500373DOI: 10.1038/s41598-018-21667-5 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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