Dataset for: A novel chitin binding mode of the chitin binding domain of chitinase A1 from Bacillus circulans WL-12 revealed by solid-state NMR
2018-09-01T09:09:10Z (GMT) by
Chitin-binding domain of chitinase A1 (ChBDChiA1) is characteristic because it binds only to insoluble crystalline chitin. While binding sites of major carbohydrate-binding modules carry multiple aromatic rings aligned on a surface, lethal mutations for ChBDChiA1 were reported only at W687, a location completely different from the site mentioned above, in spite of their similar main chain folds. Here, the structural mechanism underlying its crystalline chitin-binding was uncovered by solid-state NMR. Based on 13C- and 15N-signal assignment of microcrystalline ChBDChiA1, the chemical shift perturbation on chitin-binding was carefully examined. The perturbation was greatest at W687 and non-aromatic residues surrounding it, revealing their direct involvement in chitin-binding. These residues and Q679 should provide a novel chitin-binding platform parallel to the W687 ring.