title: Backbone chemical shifts assignments, secondary structure, and ligand binding of a family GH-19 chitinase from moss, Bryum coronatum.
abstract: Family GH19 chitinases have been recognized as important in the plant defense against fungal pathogens. However, their substrate-recognition mechanism is still unknown. We report here the first resonance assignment of NMR spectrum of a GH19 chitinase from moss, Bryum coronatum (BcChi-A). The backbone signals were nearly completely assigned, and the secondary structure was estimated based on the chemical shift values. The addition of the chitin dimer to the enzyme solution perturbed the chemical shifts of HSQC resonances of the amino acid residues forming the putative substrate-binding cleft. Further NMR analysis of the ligand binding to BcChi-A will improve understanding of the substrate-recognition mechanism of GH-19 enzymes.
authors.affiliation: Department of Advanced Bioscience, Kinki University, 3327-204, Nakamachi, Nara 631-8505, Japan.
authors.forename: Shoko
authors.initials: S
authors.lastname: Shinya
authors.forename: Takuya
authors.initials: T
authors.lastname: Nagata
authors.forename: Takayuki
authors.initials: T
authors.lastname: Ohnuma
authors.forename: Toki
authors.initials: T
authors.lastname: Taira
authors.forename: Shigenori
authors.initials: S
authors.lastname: Nishimura
authors.forename: Tamo
authors.initials: T
authors.lastname: Fukamizo
mesh_terms: D044002:Bryophyta / Q000201:enzymology*; D002688:Chitinases / Q000737:chemistry*; D008024:Ligands; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
chemical_list: D008024:Ligands; D002688:Chitinases