Characterization and crystal structure determination of β‐1,2‐mannobiose phosphorylase from Listeria innocua
Characterization and crystal structure determination of β‐1,2‐mannobiose phosphorylase from Listeria innocua
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DOI：
10.1016/j.febslet.2015.11.034
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发表时间：
2015-12
期刊：
影响因子：
3.5
通讯作者：
T. Tsuda;T. Nihira;K. Chiku;E. Suzuki;T. Arakawa;M. Nishimoto;M. Kitaoka;Hiroyuki Nakai;S. Fushinobu
中科院分区：
文献类型：
--
作者：
T. Tsuda;T. Nihira;K. Chiku;E. Suzuki;T. Arakawa;M. Nishimoto;M. Kitaoka;Hiroyuki Nakai;S. Fushinobu
糖苷水解酶家族 130 由磷酸化酶和 β-甘露糖苷水解酶组成。在这里，我们对来自无害李斯特菌 (Lin0857) 的 β-1,2-甘露二糖磷酸化酶进行了表征，并确定了其与 β-1,2-连接的甘露寡糖复合的晶体结构。 β-1,2-甘露三糖以 U 形结合，与两端的磷酸盐类似物相互作用。 Lin0857 具有通过环连接的独特二聚体结构，并且在底物进入时观察到显着的开闭环位移。 Lin0857 中独有的长环覆盖活性位点以限制口袋尺寸。提供了底物识别和磷酸解的结构基础。
Glycoside hydrolase family 130 consists of phosphorylases and hydrolases for β‐mannosides. Here, we characterized β‐1,2‐mannobiose phosphorylase fromListeria 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.