6UI4

Crystal structure of phenamacril-bound F. graminearum myosin I

Summary for 6UI4

• Entry DOI: 10.2210/pdb6ui4/pdb
• Descriptor: myosin I, Calmodulin, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: myosin i, phenamcril, atpase activity, fungicide, f. graminearum, hydrolase
• Biological source: Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus); More
• Total number of polymer chains: 2
• Total formula weight: 96405.31

Authors

Zhou, Y.,Zhou, X.E.,Gong, Y.,Zhu, Y.,Xu, H.E.,Zhou, M.,Melcher, K.,Zhang, F. (deposition date: 2019-09-30, release date: 2020-03-25, Last modification date: 2024-10-23)

Primary citation

Zhou, Y.,Zhou, X.E.,Gong, Y.,Zhu, Y.,Cao, X.,Brunzelle, J.S.,Xu, H.E.,Zhou, M.,Melcher, K.,Zhang, F.
Structural basis of Fusarium myosin I inhibition by phenamacril.
Plos Pathog., 16:e1008323-e1008323, 2020

PubMed Abstract: Fusarium is a genus of filamentous fungi that includes species that cause devastating diseases in major staple crops, such as wheat, maize, rice, and barley, resulting in severe yield losses and mycotoxin contamination of infected grains. Phenamacril is a novel fungicide that is considered environmentally benign due to its exceptional specificity; it inhibits the ATPase activity of the sole class I myosin of only a subset of Fusarium species including the major plant pathogens F. graminearum, F. asiaticum and F. fujikuroi. To understand the underlying mechanisms of inhibition, species specificity, and resistance mutations, we have determined the crystal structure of phenamacril-bound F. graminearum myosin I. Phenamacril binds in the actin-binding cleft in a new allosteric pocket that contains the central residue of the regulatory Switch 2 loop and that is collapsed in the structure of a myosin with closed actin-binding cleft, suggesting that pocket occupancy blocks cleft closure. We have further identified a single, transferable phenamacril-binding residue found exclusively in phenamacril-sensitive myosins to confer phenamacril selectivity.

PubMed: 32163521
DOI: 10.1371/journal.ppat.1008323

Experimental method

X-RAY DIFFRACTION (2.65 Å)