维生素B12
半胱氨酸
科林
化学
生物化学
配体(生物化学)
膜
转运蛋白
立体化学
受体
酶
作者
S. Rempel,E. Colucci,Jan‐Willem De Gier,Albert Guskov,Dirk Jan Slotboom
标识
DOI:10.1038/s41467-018-05441-9
摘要
Uptake of vitamin B12 is essential for many prokaryotes, but in most cases the membrane proteins involved are yet to be identified. We present the biochemical characterization and high-resolution crystal structure of BtuM, a predicted bacterial vitamin B12 uptake system. BtuM binds vitamin B12 in its base-off conformation, with a cysteine residue as axial ligand of the corrin cobalt ion. Spectroscopic analysis indicates that the unusual thiolate coordination allows for decyanation of vitamin B12. Chemical modification of the substrate is a property other characterized vitamin B12-transport proteins do not exhibit.
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