| Structural highlights
Function
BMBP_LISIN Catalyzes the reversible phosphorolysis of 1,2-beta-oligomannan (PubMed:26632508). In phosphorolytic reactions, prefers beta-1,2-mannobiose (beta-1,2-Man2) as substrate, but can also use beta-1,2-mannotriose (PubMed:26632508).[1]
Publication Abstract from PubMed
Glycoside hydrolase family 130 consists of phosphorylases and hydrolases for beta-mannosides. Here, we characterized beta-1,2-mannobiose phosphorylase from Listeria innocua (Lin0857) and determined its crystal structures complexed with beta-1,2-linked mannooligosaccharides. beta-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.
Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua.,Tsuda T, Nihira T, Chiku K, Suzuki E, Arakawa T, Nishimoto M, Kitaoka M, Nakai H, Fushinobu S FEBS Lett. 2015 Dec 21;589(24 Pt B):3816-21. doi: 10.1016/j.febslet.2015.11.034. , Epub 2015 Nov 26. PMID:26632508[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2015 Dec 21;589(24 Pt B):3816-21. doi: 10.1016/j.febslet.2015.11.034. , Epub 2015 Nov 26. PMID:26632508 doi:http://dx.doi.org/10.1016/j.febslet.2015.11.034
- ↑ 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. 2015 Dec 21;589(24 Pt B):3816-21. doi: 10.1016/j.febslet.2015.11.034. , Epub 2015 Nov 26. PMID:26632508 doi:http://dx.doi.org/10.1016/j.febslet.2015.11.034
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