5IAZ
The C-terminal domain of rice beta-galactosidase 1
Summary for 5IAZ
| Entry DOI | 10.2210/pdb5iaz/pdb |
| NMR Information | BMRB: 30020 |
| Descriptor | beta-galactosidase 1 (1 entity in total) |
| Functional Keywords | glycoside hydrolase, exoglycosidase, beta-sandwich, hydrolase |
| Biological source | Oryza sativa subsp. indica (Rice) |
| Total number of polymer chains | 1 |
| Total formula weight | 13029.78 |
| Authors | Rimlumduan, T.,Hua, Y.-l.,Tanaka, T.,Ketudat-Cairns, J.R. (deposition date: 2016-02-22, release date: 2016-08-10, Last modification date: 2024-11-06) |
| Primary citation | Rimlumduan, T.,Hua, Y.-L.,Tanaka, T.,Ketudat Cairns, J.R. Structure of a plant beta-galactosidase C-terminal domain Biochim.Biophys.Acta, 1864:1411-1418, 2016 Cited by PubMed Abstract: Most plant β-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.) β-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 β-strands and one α-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, β-1,4-d-galactobiose and raffinose could not be observed in NMR experiments. PubMed: 27451952DOI: 10.1016/j.bbapap.2016.07.005 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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