4dyg

Crystal Structure of a Family GH-19 Chitinase from rye seeds in complex with (GlcNAc)4

spinqualitylabelsall models 4dyg, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4dyg is a 2 chain structure with sequence from Secale cereale. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: MES, NAG, SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CHIC_SECCE Defense against chitin containing fungal pathogens. Binds the hyphal tips of fungi and degrades nascent chitin. Publication Abstract from PubMed Substrate-binding mode of a 26-kDa GH19 chitinase from rye, Secale cereale, seeds (RSC-c) was investigated by crystallography, site-directed mutagenesis, and NMR spectroscopy. The crystal structure of RSC-c in a complex with an N-acetylglucosamine tetramer, (GlcNAc)(4) , was successfully solved, and revealed the binding mode of the tetramer to an aglycon binding site, subsites +1, +2, +3, and +4. This is the first crystallographic data showing the oligosaccharide-binding mode of a family GH-19 chitinase. From an HPLC analysis of the enzymatic reaction products, mutation of Trp72 to alanine was found to affect the product distribution obtained from the substrate, p-nitrophenyl penta-N-acetyl-beta-chitopentaoside. The mutational experiments confirmed the crystallographic finding that the Trp72 side chain interacts with the +4 moiety of the bound substrate. To further confirm the crystallographic data, the binding experiments were also conducted in solution using NMR spectroscopy. Several signals in the (1) H-(15) N HSQC spectrum of the stable isotope-labeled RSC-c were affected upon the addition of (GlcNAc)(4) . Signal assignments revealed that most signals responsive to the addition of (GlcNAc)(4) are derived from amino acids located at the surface of the aglycon-binding site. The binding mode deduced from NMR binding experiments in solution was well consistent with that from the crystal structure. (c) 2012 The Authors Journal compilation (c) 2012 FEBS. Crystal structure and chitin oligosaccharide-binding mode of a "loopful" family GH19 chitinase from rye, Secale cereal, seeds.,Ohnuma T, Numata T, Osawa T, Inanaga H, Okazaki Y, Shinya S, Kondo K, Fukuda T, Fukamizo T FEBS J. 2012 Jul 25. doi: 10.1111/j.1742-4658.2012.08723.x. PMID:22831795 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chitinase 3D structures

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