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Publication Abstract from PubMed

Most plant beta-galactosidases, which belong to glycoside hydrolase family 35, have a C-terminal domain homologous to animal galactose and rhamnose-binding lectins. To investigate the structure and function of this domain, the C-terminal domain of the rice (Oryza sativa L.) beta-galactosidase 1 (OsBGal1 Cter) was expressed in Escherichia coli and purified to homogeneity. The free OsBGal1 Cter is monomeric with a native molecular weight of 15kDa. NMR spectroscopy indicated that OsBGal1 Cter comprises five beta-strands and one alpha-helix. The structure of this domain is similar to lectin domains from animals, but loops A and C of OsBGal1 Cter are longer than the corresponding loops from related animal lectins with known structures. In addition, loop A of OsBGal1 Cter was not well defined, suggesting it is flexible. Although OsBGal1 Cter was predicted to be a galactose/rhamnose-binding domain, binding with rhamnose, galactose, glucose, beta-1,4-d-galactobiose and raffinose could not be observed in NMR experiments.

Structure of a plant beta-galactosidase C-terminal domain.,Rimlumduan T, Hua YL, Tanaka T, Ketudat Cairns JR Biochim Biophys Acta. 2016 Jul 22;1864(10):1411-1418. doi:, 10.1016/j.bbapap.2016.07.005. PMID:27451952^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.