Three-dimensional structure and properties of the giant reed ( Arundo donax ) lectin (ADL)

PERDUCA, MASSIMILIANO; BOVI, MICHELE; DESTEFANIS, LAURA; NADALI, DIVINA; FIN, LAURA; PAROLINI, FRANCESCA; SORIO, DANIELA; CARRIZO, MARIA E; MONACO, HUGO L

GLYCOBIOLOGY

Oxford University Press

Año: 2021

0959-6658

rundo donax lectin (ADL) is a 170 amino acid protein that can be purified from the rhizomes of the giant reed or giant cane exploiting its selective binding to chitin followed by elution with N-acetyl glucosamine. The lectin is listed in the UniProt server, the largest protein sequence database, as an uncharacterized protein with chitin-binding domains (A0A0A9P802).This paper reports the purification, three-dimensional structure and ligand-binding properties of ADL. The lectin is a homodimer in which the two protomers are linked by two disulphide bridges. Each polypeptide chain presents four carbohydrate-binding modules that belong to family 18 (CBM18). A high degree of sequence similarity is observed among the modules present in each protomer. We have determined the X-ray structure of the apo-protein to a resolution of 1.70 Å. The carbohydrate-binding modules, that span a sequence of approximately 40 amino acids, present four internal disulfide bridges a very short antiparallel centr