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Characterization and crystal structure determination of β‐1,2‐mannobiose phosphorylase from Listeria innocua
Author(s) -
Tsuda Tomohiro,
Nihira Takanori,
Chiku Kazuhiro,
Suzuki Erika,
Arakawa Takatoshi,
Nishimoto Mamoru,
Kitaoka Motomitsu,
Nakai Hiroyuki,
Fushinobu Shinya
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.11.034
Subject(s) - listeria , characterization (materials science) , chemistry , glycogen phosphorylase , biochemistry , enzyme , listeria monocytogenes , materials science , biology , bacteria , nanotechnology , genetics
Glycoside hydrolase family 130 consists of phosphorylases and hydrolases for β‐mannosides. Here, we characterized β‐1,2‐mannobiose phosphorylase from Listeria innocua (Lin0857) and determined its crystal structures complexed with β‐1,2‐linked mannooligosaccharides. β‐1,2‐Mannotriose was bound in a U‐shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, and a significant open–close loop displacement was observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size. A structural basis for substrate recognition and phosphorolysis was provided.