Molybdenum-binding protein (Mop) (Mop)

The Molybdenum-binding protein (Mop), also known as a molbindin, is a small (approximately 7 kDa) protein found in various bacteria, including Haemophilus influenzae, Sporomusa ovata, and Rhodobacter capsulatus [1, 2, 5]. It typically assembles into a highly symmetric hexameric complex, known as the Mop hexamer, which is stabilized by the binding of molybdate or tungstate oxyanions [1, 5, 8]. The primary biological function of the Mop hexamer is to facilitate molybdenum homeostasis and storage within the bacterial cell, ensuring the availability of this essential trace element for the synthesis of molybdenum-containing enzymes (molybdoenzymes) [1, 2, 3]. While it plays a crucial role in bacterial metabolism and survival, it is not currently recognized as a primary therapeutic target for human medicine, and no drugs are known to specifically interact with this protein complex [1, 11]. Its structure is characterized by an oligonucleotide/oligosaccharide-binding (OB) fold, which is also found in the molybdate-binding domains of other proteins like the transcriptional regulator ModE [5, 8].

Other names

MolbindinMolybdenum-binding proteinMop proteinMop hexamer