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Characterization of crystal structure and key residues of Aspergillus fumigatus nucleoside diphosphate kinase
- Source :
- Biochemical and Biophysical Research Communications. 511:148-153
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
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.
- Subjects :
- Models, Molecular
0301 basic medicine
Hot Temperature
Protein Conformation
Biophysics
Crystallography, X-Ray
medicine.disease_cause
Biochemistry
Aspergillus fumigatus
03 medical and health sciences
0302 clinical medicine
Tetramer
Enzyme Stability
medicine
Aspergillosis
Humans
Transferase
Kinase activity
skin and connective tissue diseases
Molecular Biology
Protein secondary structure
chemistry.chemical_classification
Mutation
biology
Cell Biology
biology.organism_classification
Nucleoside-diphosphate kinase
Amino acid
030104 developmental biology
chemistry
Nucleoside-Diphosphate Kinase
030220 oncology & carcinogenesis
Protein Multimerization
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 511
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....5ebf28ccbff7e923d276b0fe94d8077f