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-Structure paper
タイトル | Structural basis for directional chitin biosynthesis. |
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ジャーナル・号・ページ | Nature, Vol. 610, Issue 7931, Page 402-408, Year 2022 |
掲載日 | 2022年9月21日 |
![]() | Wei Chen / Peng Cao / Yuansheng Liu / Ailing Yu / Dong Wang / Lei Chen / Rajamanikandan Sundarraj / Zhiguang Yuchi / Yong Gong / Hans Merzendorfer / Qing Yang / ![]() ![]() |
PubMed 要旨 | Chitin, the most abundant aminopolysaccharide in nature, is an extracellular polymer consisting of N-acetylglucosamine (GlcNAc) units. The key reactions of chitin biosynthesis are catalysed by chitin ...Chitin, the most abundant aminopolysaccharide in nature, is an extracellular polymer consisting of N-acetylglucosamine (GlcNAc) units. The key reactions of chitin biosynthesis are catalysed by chitin synthase, a membrane-integrated glycosyltransferase that transfers GlcNAc from UDP-GlcNAc to a growing chitin chain. However, the precise mechanism of this process has yet to be elucidated. Here we report five cryo-electron microscopy structures of a chitin synthase from the devastating soybean root rot pathogenic oomycete Phytophthora sojae (PsChs1). They represent the apo, GlcNAc-bound, nascent chitin oligomer-bound, UDP-bound (post-synthesis) and chitin synthase inhibitor nikkomycin Z-bound states of the enzyme, providing detailed views into the multiple steps of chitin biosynthesis and its competitive inhibition. The structures reveal the chitin synthesis reaction chamber that has the substrate-binding site, the catalytic centre and the entrance to the polymer-translocating channel that allows the product polymer to be discharged. This arrangement reflects consecutive key events in chitin biosynthesis from UDP-GlcNAc binding and polymer elongation to the release of the product. We identified a swinging loop within the chitin-translocating channel, which acts as a 'gate lock' that prevents the substrate from leaving while directing the product polymer into the translocating channel for discharge to the extracellular side of the cell membrane. This work reveals the directional multistep mechanism of chitin biosynthesis and provides a structural basis for inhibition of chitin synthesis. |
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手法 | EM (単粒子) |
解像度 | 3.1 - 3.9 Å |
構造データ | EMDB-32545, PDB-7wjm: EMDB-32546, PDB-7wjn: EMDB-32547, PDB-7wjo: EMDB-32917, PDB-7x05: EMDB-32918, PDB-7x06: |
化合物 | ![]() ChemComp-UD1: ![]() ChemComp-MN: ![]() ChemComp-BGI: ![]() ChemComp-UDP: ![]() ChemComp-MG: |
由来 |
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![]() | TRANSFERASE / carbohydate / biosynthetic protein / membrane protein |