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-Structure paper
Title | Structure, catalysis, chitin transport, and selective inhibition of chitin synthase. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 4776, Year 2023 |
Publish date | Aug 8, 2023 |
Authors | Dan-Dan Chen / Zhao-Bin Wang / Le-Xuan Wang / Peng Zhao / Cai-Hong Yun / Lin Bai / |
PubMed Abstract | Chitin is one of the most abundant natural biopolymers and serves as a critical structural component of extracellular matrices, including fungal cell walls and insect exoskeletons. As a linear ...Chitin is one of the most abundant natural biopolymers and serves as a critical structural component of extracellular matrices, including fungal cell walls and insect exoskeletons. As a linear polymer of β-(1,4)-linked N-acetylglucosamine, chitin is synthesized by chitin synthases, which are recognized as targets for antifungal and anti-insect drugs. In this study, we determine seven different cryo-electron microscopy structures of a Saccharomyces cerevisiae chitin synthase in the absence and presence of glycosyl donor, acceptor, product, or peptidyl nucleoside inhibitors. Combined with functional analyses, these structures show how the donor and acceptor substrates bind in the active site, how substrate hydrolysis drives self-priming, how a chitin-conducting transmembrane channel opens, and how peptidyl nucleoside inhibitors inhibit chitin synthase. Our work provides a structural basis for understanding the function and inhibition of chitin synthase. |
External links | Nat Commun / PubMed:37553334 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.6 - 3.64 Å |
Structure data | EMDB-36855, PDB-8k3p: EMDB-36856, PDB-8k3q: EMDB-36857, PDB-8k3r: EMDB-36859, PDB-8k3t: EMDB-36861, PDB-8k3u: EMDB-36862, PDB-8k3v: EMDB-36863, PDB-8k3w: EMDB-36864, PDB-8k3x: |
Chemicals | ChemComp-POV: ChemComp-VDG: ChemComp-MG: ChemComp-UDP: ChemComp-NAG: ChemComp-UD1: ChemComp-BGI: |
Source |
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Keywords | ANTIFUNGAL PROTEIN/INHIBITOR / ANTIFUNGAL PROTEIN-INHIBITOR complex |