5B0R
Beta-1,2-Mannobiose phosphorylase from Listeria innocua - beta-1,2-mannobiose complex
Summary for 5B0R
Entry DOI | 10.2210/pdb5b0r/pdb |
Related | 5B0P 5B0Q 5B0S |
Descriptor | Lin0857 protein, beta-D-mannopyranose-(1-2)-beta-D-mannopyranose, SULFATE ION, ... (6 entities in total) |
Functional Keywords | glycoside phosphorylase, transferase |
Biological source | Listeria innocua Clip11262 |
Total number of polymer chains | 2 |
Total formula weight | 84432.23 |
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 Cited by 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: 26632508DOI: 10.1016/j.febslet.2015.11.034 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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