June 5, 2017

The α-N-acetylgalactosaminidase from the probiotic bacterium Bifidobacterium bifidum (NagBb) belongs to the glycoside hydrolase (GH) family 129 and hydrolyzes the glycosidic bond of Tn antigen (GalNAcα1-Ser/Thr). NagBb is involved in assimilation of O-glycans on mucin glycoproteins by B. bifidum in the human gastrointestinal tract, but its catalytic mechanism has remained elusive because of a lack of sequence homology around putative catalytic residues and of other structural information. Here we report the X-ray crystal structure of NagBb, representing the first GH129 family structure, solved by the single-wavelength anomalous dispersion method based on sulfur atoms of the native protein. ……

  For details, please refer to the following link  

http://www.jbc.org/content/early/2017/05/25/jbc.M117.777391

Paper Information

authors
Mayo Sato*1, Dorothee Liebschner*2, Yusuke Yamada*3, Naohiro Matsugaki*3, Takatoshi Arakawa*1, Siobhan S. Wills*4, Mitchell Hattie*4, Keith A. Stubbs*4, Tasuku Ito*5, Toshiya Senda*3, Hisashi Ashida*6 and Shinya Fushinobu*1

Author Affiliations
 *1 The University of Tokyo, Japan;
 *2 Lawrence Berkeley National Laboratory, United States;
 *3 High Energy Accelerator Research Organization, Japan;
 *4 The University of Western Australia, Australia;
 *5 Yamada Apiculture Center Inc., Japan;
 *6 Kindai University, Japan

DOI: 10.1074/jbc.M117.777391

http://www.jbc.org/content/early/2017/05/25/jbc.M117.777391