6AGY
Aspergillus fumigatus Af293 NDK
Summary for 6AGY
| Entry DOI | 10.2210/pdb6agy/pdb |
| Descriptor | Nucleoside diphosphate kinase (2 entities in total) |
| Functional Keywords | kinase, transferase |
| Biological source | Aspergillus fumigatus Af293 (Aspergillus fumigatus) |
| Total number of polymer chains | 1 |
| Total formula weight | 18023.62 |
| Authors | |
| Primary citation | Hu, Y.,Jia, X.,Lu, Z.,Han, L. Characterization of crystal structure and key residues of Aspergillus fumigatus nucleoside diphosphate kinase. Biochem. Biophys. Res. Commun., 511:148-153, 2019 Cited by PubMed Abstract: Aspergillus fumigatus is a major pathogen of invasive pulmonary aspergillosis with high mortality rate. The nucleoside diphosphate kinase of A. fumigatus, AfNDK (also called SwoH) is essential for its viability, however, its structural characteristic was unknown. In this study, we solved the crystal structure of AfNDK and found that it exists predominantly in form of tetramer in solution. Oligomeric form rather than dimeric form was essential for its kinase activity. The Arg30 and the C terminal amino acids were crucial for dimer-dimer interaction and the viability of A. fumigatus. Mutation V83F might make the secondary structure α5 helix protrude outward so that the whole protein structure became unstable at higher temperature, which might subsequently result to the inviability of A. fumigatus under 44 °C. In conclusion, the crystal structure of AfNDK was for the first time analyzed and the stability of the tetrameric form with dimer-dimer interaction were crucial for its function in A. fumigatus. PubMed: 30773256DOI: 10.1016/j.bbrc.2019.01.126 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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