Vitamin B12-binding protein (BtuF) (BtuF)

BtuF is a periplasmic binding protein in Gram-negative bacteria, such as Escherichia coli, that plays a critical role in the high-affinity uptake of Vitamin B12 (cobalamin) [1, 4]. It is a key component of the BtuCDF ABC transporter system, where it captures B12 in the periplasmic space and delivers it to the BtuCD membrane complex for ATP-dependent transport into the cytoplasm [2, 9]. Structurally, BtuF consists of two lobes that close around the B12 molecule, a process often described by the Venus flytrap mechanism [7, 8]. Because Vitamin B12 is an essential cofactor for various bacterial metabolic pathways, BtuF is considered a promising target for the development of narrow-spectrum antibacterial agents that aim to starve pathogens of vital nutrients [11, 21]. While no clinical drugs currently target BtuF, research into small-molecule inhibitors and nanobodies is ongoing to combat antibiotic-resistant infections [21, 27].

Other names

yadTVitamin B12 ABC transporter periplasmic binding proteinCobalamin-binding proteinPeriplasmic cobalamin-binding protein

Competitive inhibition of Vitamin B12 binding or steric blocking of the interaction between the BtuF protein and the BtuCD transmembrane transporter complex.