Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for directional chitin biosynthesis.
Journal, issue, pages	Nature, Vol. 610, Issue 7931, Page 402-408, Year 2022
Publish date	Sep 21, 2022
Authors	Wei Chen / Peng Cao / Yuansheng Liu / Ailing Yu / Dong Wang / Lei Chen / Rajamanikandan Sundarraj / Zhiguang Yuchi / Yong Gong / Hans Merzendorfer / Qing Yang /
PubMed Abstract	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.
External links	Nature / PubMed:36131020 / PubMed Central
Methods	EM (single particle)
Resolution	3.1 - 3.9 Å
Structure data	32545 7wjm EMDB-32545, PDB-7wjm: CryoEM structure of chitin synthase 1 from Phytophthora sojae Method: EM (single particle) / Resolution: 3.3 Å 32546 7wjn EMDB-32546, PDB-7wjn: CryoEM structure of chitin synthase 1 mutant E495A from Phytophthora sojae complexed with UDP-GlcNAc Method: EM (single particle) / Resolution: 3.3 Å 32547 7wjo EMDB-32547, PDB-7wjo: CryoEM structure of chitin synthase 1 from Phytophthora sojae complexed with nikkomycin Z Method: EM (single particle) / Resolution: 3.2 Å 32917 7x05 EMDB-32917, PDB-7x05: CryoEM structure of chitin synthase 1 from Phytophthora sojae complexed with the nascent chitooligosaccharide Method: EM (single particle) / Resolution: 3.9 Å 32918 7x06 EMDB-32918, PDB-7x06: CryoEM structure of chitin synthase 1 from Phytophthora sojae complexed with UDP Method: EM (single particle) / Resolution: 3.1 Å
Chemicals	ChemComp-UD1: URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE 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) / medication, antifungalYM / Nikkomycin ChemComp-UDP: URIDINE-5'-DIPHOSPHATE / UDPYM / Uridine diphosphate ChemComp-MG: Unknown entry
Source	phytophthora sojae strain p6497 (eukaryote)
Keywords	TRANSFERASE / carbohydate / biosynthetic protein / membrane protein