5B0P

Beta-1,2-Mannobiose phosphorylase from Listeria innocua - glycerol complex

Summary for 5B0P

• Entry DOI: 10.2210/pdb5b0p/pdb
• Related: 5B0Q 5B0R 5B0S
• Descriptor: Lin0857 protein, SULFATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: glycoside phosphorylase, transferase
• Biological source: Listeria innocua Clip11262
• Total number of polymer chains: 2
• Total formula weight: 84042.05

Authors

Tsuda, T.,Arakawa, T.,Fushinobu, S. (deposition date: 2015-11-02, release date: 2015-12-02, Last modification date: 2023-11-08)

Primary citation

Tsuda, T.,Nihira, T.,Chiku, K.,Suzuki, E.,Arakawa, T.,Nishimoto, M.,Kitaoka, M.,Nakai, H.,Fushinobu, S.
Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua
Febs Lett., 589:3816-3821, 2015

PubMed Abstract: 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.

PubMed: 26632508
DOI: 10.1016/j.febslet.2015.11.034

Experimental method

X-RAY DIFFRACTION (1.9 Å)