8K3X
S. cerevisiae Chs1 in complex with Nikkomycin Z
8K3X の概要
エントリーDOI | 10.2210/pdb8k3x/pdb |
EMDBエントリー | 36864 |
分子名称 | Chitin synthase 1, (2S)-{[(2S,3S,4S)-2-amino-4-hydroxy-4-(5-hydroxypyridin-2-yl)-3-methylbutanoyl]amino}[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxyoxolan-2-yl]acetic acid (non-preferred name) (2 entities in total) |
機能のキーワード | antifungal protein-inhibitor complex, antifungal protein/inhibitor |
由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 260993.16 |
構造登録者 | |
主引用文献 | Chen, D.D.,Wang, Z.B.,Wang, L.X.,Zhao, P.,Yun, C.H.,Bai, L. Structure, catalysis, chitin transport, and selective inhibition of chitin synthase. Nat Commun, 14:4776-4776, 2023 Cited by 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 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. PubMed: 37553334DOI: 10.1038/s41467-023-40479-4 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.86 Å) |
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