EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Structural basis for directional chitin biosynthesis.
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
著者	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.
リンク	Nature / PubMed:36131020 / PubMed Central
手法	EM (単粒子)
解像度	3.1 - 3.9 Å
構造データ	32545 7wjm EMDB-32545, PDB-7wjm: CryoEM structure of chitin synthase 1 from Phytophthora sojae 手法: EM (単粒子) / 解像度: 3.3 Å 32546 7wjn EMDB-32546, PDB-7wjn: CryoEM structure of chitin synthase 1 mutant E495A from Phytophthora sojae complexed with UDP-GlcNAc 手法: EM (単粒子) / 解像度: 3.3 Å 32547 7wjo EMDB-32547, PDB-7wjo: CryoEM structure of chitin synthase 1 from Phytophthora sojae complexed with nikkomycin Z 手法: EM (単粒子) / 解像度: 3.2 Å 32917 7x05 EMDB-32917, PDB-7x05: CryoEM structure of chitin synthase 1 from Phytophthora sojae complexed with the nascent chitooligosaccharide 手法: EM (単粒子) / 解像度: 3.9 Å 32918 7x06 EMDB-32918, PDB-7x06: CryoEM structure of chitin synthase 1 from Phytophthora sojae complexed with UDP 手法: EM (単粒子) / 解像度: 3.1 Å
化合物	ChemComp-UD1: URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE / UDP-GlcNAc ChemComp-MN: Unknown entry ChemComp-BGI: (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) / ニッコマイシンZ / 薬剤, 抗真菌剤YM ChemComp-UDP: URIDINE-5'-DIPHOSPHATE / UDP / UDPYM ChemComp-MG: Unknown entry / マグネシウムジカチオン
由来	phytophthora sojae strain p6497 (真核生物)
キーワード	TRANSFERASE / carbohydate / biosynthetic protein / membrane protein