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6K3H

Crystallographic Analysis of Nucleoside Diphosphate Kinase (NDK) from Aspergillus Flavus

Summary for 6K3H
Entry DOI10.2210/pdb6k3h/pdb
DescriptorNucleoside diphosphate kinase (1 entity in total)
Functional Keywordsnucleoside diphosphate kinase, aspergillus flavus, filamentous fungi, transferase
Biological sourceAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Total number of polymer chains24
Total formula weight412480.22
Authors
Wang, Y.,Wang, S.,Wang, S.H. (deposition date: 2019-05-18, release date: 2019-07-03, Last modification date: 2023-11-22)
Primary citationWang, Y.,Wang, S.,Nie, X.,Yang, K.,Xu, P.,Wang, X.,Liu, M.,Yang, Y.,Chen, Z.,Wang, S.
Molecular and structural basis of nucleoside diphosphate kinase-mediated regulation of spore and sclerotia development in the fungusAspergillus flavus.
J.Biol.Chem., 294:12415-12431, 2019
Cited by
PubMed Abstract: The fundamental biological function of nucleoside diphosphate kinase (NDK) is to catalyze the reversible exchange of the γ-phosphate between nucleoside triphosphate (NTP) and nucleoside diphosphate (NDP). This kinase also has functions that extend beyond its canonically defined enzymatic role as a phosphotransferase. However, the role of NDK in filamentous fungi, especially in (), is not yet known. Here we report that has two NDK-encoding gene copies as assessed by qPCR. Using gene-knockout and complementation experiments, we found that AfNDK regulates spore and sclerotia development and is involved in plant virulence as assessed in corn and peanut seed-based assays. An antifungal test with the inhibitor azidothymidine suppressed AfNDK activity and prevented spore production and sclerotia formation in , confirming AfNDK's regulatory functions. Crystallographic analysis of AfNDK, coupled with site-directed mutagenesis experiments, revealed three residues (Arg-104, His-117, and Asp-120) as key sites that contribute to spore and sclerotia development. These results not only enrich our knowledge of the regulatory role of this important protein in , but also provide insights into the prevention of infection in plants and seeds, as well as into the structural features relevant for future antifungal drug development.
PubMed: 31243100
DOI: 10.1074/jbc.RA119.007505
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.179 Å)
Structure validation

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