Crystal structures of starch binding domain from Rhizopus oryzae glucoamylase in complex with isomaltooligosaccharide: Insights into polysaccharide binding mechanism of CBM21 family

2013 ◽  
Vol 82 (6) ◽  
pp. 1079-1085 ◽  
Author(s):  
Chen-Hsi Chu ◽  
Kun-Mou Li ◽  
Shih-Wei Lin ◽  
Margaret Dah-Tsyr Chang ◽  
Ting-Ying Jiang ◽  
...  
2008 ◽  
Vol 416 (1) ◽  
pp. 27-36 ◽  
Author(s):  
Jung-Yu Tung ◽  
Margaret Dah-Tsyr Chang ◽  
Wei-I Chou ◽  
Yen-Yi Liu ◽  
Yi-Hung Yeh ◽  
...  

GA (glucoamylase) hydrolyses starch and polysaccharides to β-D-glucose. RoGA (Rhizopus oryzae GA) consists of two functional domains, an N-terminal SBD (starch-binding domain) and a C-terminal catalytic domain, which are connected by an O-glycosylated linker. In the present study, the crystal structures of the SBD from RoGA (RoGACBM21) and the complexes with β-cyclodextrin (SBD–βCD) and maltoheptaose (SBD–G7) were determined. Two carbohydrate binding sites, I (Trp47) and II (Tyr32), were resolved and their binding was co-operative. Besides the hydrophobic interaction, two unique polyN loops comprising consecutive asparagine residues also participate in the sugar binding. A conformational change in Tyr32 was observed between unliganded and liganded SBDs. To elucidate the mechanism of polysaccharide binding, a number of mutants were constructed and characterized by a quantitative binding isotherm and Scatchard analysis. A possible binding path for long-chain polysaccharides in RoGACBM21 was proposed.


2017 ◽  
Vol 68 ◽  
pp. 78-91 ◽  
Author(s):  
Prabodh Ranjan ◽  
Sivakumar Prasanth Kumar ◽  
Vijayakrishna Kari ◽  
Prakash Chandra Jha

2018 ◽  
Vol 10 (3) ◽  
pp. 243-247
Author(s):  
Saara Laulumaa ◽  
Kathrine Voigt Hansen ◽  
Magdalena Masternak ◽  
Thomas Drapier ◽  
Pierre Francotte ◽  
...  

PLoS ONE ◽  
2012 ◽  
Vol 7 (7) ◽  
pp. e41131 ◽  
Author(s):  
Ting-Ying Jiang ◽  
Yuan-Pei Ci ◽  
Wei-I Chou ◽  
Yuan-Chuan Lee ◽  
Yuh-Ju Sun ◽  
...  

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