scholarly journals Crystal structure of the N-terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea

FEBS Letters ◽  
2013 ◽  
Vol 587 (14) ◽  
pp. 2193-2198 ◽  
Author(s):  
Takatsugu Miyazaki ◽  
Makoto Yoshida ◽  
Mizuki Tamura ◽  
Yutaro Tanaka ◽  
Kiwamu Umezawa ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Coprinopsis Cinerea ◽  
Terminal Domain ◽  
Hydrolase Family

Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea

FEBS Journal ◽  
2010 ◽  
Vol 277 (6) ◽  
pp. 1532-1542 ◽  
Author(s):  
Yuan Liu ◽  
Makoto Yoshida ◽  
Yuma Kurakata ◽  
Takatsugu Miyazaki ◽  
Kiyohiko Igarashi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Coprinopsis Cinerea ◽  
Hydrolase Family

scholarly journals Crystal Structure and Mutational Analysis of Isomalto-dextranase, a Member of Glycoside Hydrolase Family 27

2015 ◽  
Vol 290 (43) ◽  
pp. 26339-26349 ◽  
Author(s):  
Yuka Okazawa ◽  
Takatsugu Miyazaki ◽  
Gaku Yokoi ◽  
Yuichi Ishizaki ◽  
Atsushi Nishikawa ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Glycoside Hydrolase ◽  
Mutational Analysis ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family

scholarly journals The structure of PfGH50B, an agarase from the marine bacterium Pseudoalteromonas fuliginea PS47

2020 ◽  
Vol 76 (9) ◽  
pp. 422-427
Author(s):  
Benjamin Pluvinage ◽  
Craig S. Robb ◽  
Roderick Jeffries ◽  
Alisdair B. Boraston
Keyword(s):  
Glycoside Hydrolase ◽  
Marine Bacterium ◽  
Structural Features ◽  
Degree Of Polymerization ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
X Ray ◽  
Terminal Domain ◽  
Polysaccharide Utilization Locus ◽  
Hydrolase Family

The recently identified marine bacterium Pseudoalteromonas fuliginea sp. PS47 possesses a polysaccharide-utilization locus dedicated to agarose degradation. In particular, it contains a gene (locus tag EU509_06755) encoding a β-agarase that belongs to glycoside hydrolase family 50 (GH50), PfGH50B. The 2.0 Å resolution X-ray crystal structure of PfGH50B reveals a rare complex multidomain fold that was found in two of the three previously determined GH50 structures. The structure comprises an N-terminal domain with a carbohydrate-binding module (CBM)-like fold fused to a C-terminal domain by a rigid linker. The CBM-like domain appears to function by extending the catalytic groove of the enzyme. Furthermore, the PfGH50B structure highlights key structural features in the mobile loops that may function to restrict the degree of polymerization of the neoagaro-oligosaccharide products and the enzyme processivity.

scholarly journals Crystal structure of β-L-arabinobiosidase belonging to glycoside hydrolase family 121

PLoS ONE ◽  
2020 ◽  
Vol 15 (6) ◽  
pp. e0231513 ◽  
Author(s):  
Keita Saito ◽  
Alexander Holm Viborg ◽  
Shiho Sakamoto ◽  
Takatoshi Arakawa ◽  
Chihaya Yamada ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family
Sign in / Sign up

Export Citation Format

Share Document