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5B0R

Beta-1,2-Mannobiose phosphorylase from Listeria innocua - beta-1,2-mannobiose complex

Summary for 5B0R
Entry DOI10.2210/pdb5b0r/pdb
Related5B0P 5B0Q 5B0S
DescriptorLin0857 protein, beta-D-mannopyranose-(1-2)-beta-D-mannopyranose, SULFATE ION, ... (6 entities in total)
Functional Keywordsglycoside phosphorylase, transferase
Biological sourceListeria innocua Clip11262
Total number of polymer chains2
Total formula weight84432.23
Authors
Tsuda, T.,Arakawa, T.,Fushinobu, S. (deposition date: 2015-11-02, release date: 2015-12-02, Last modification date: 2023-11-08)
Primary citationTsuda, 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: 26632508
DOI: 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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数据于2024-11-06公开中

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