5IAZ

The C-terminal domain of rice beta-galactosidase 1

5IAZ の概要

• エントリーDOI: 10.2210/pdb5iaz/pdb
• NMR情報: BMRB: 30020
• 分子名称: beta-galactosidase 1 (1 entity in total)
• 機能のキーワード: glycoside hydrolase, exoglycosidase, beta-sandwich, hydrolase
• 由来する生物種: Oryza sativa subsp. indica (Rice)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13029.78

構造登録者

Rimlumduan, T.,Hua, Y.-l.,Tanaka, T.,Ketudat-Cairns, J.R. (登録日: 2016-02-22, 公開日: 2016-08-10, 最終更新日: 2024-11-06)

主引用文献

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

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: 27451952
DOI: 10.1016/j.bbapap.2016.07.005

実験手法

SOLUTION NMR