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substrate-binding domain-containing protein
This family includes bacterial extracellular solute-binding proteins. (from Pfam)
ABC transporter substrate-binding protein
extracellular solute-binding protein
This family also includes the bacterial extracellular solute-binding protein family POTD/POTF. [1]. 2002054. The 2.3-A resolution structure of the maltose- or. maltodextrin-binding protein, a primary receptor of bacterial. active transport and chemotaxis.. Spurlino JC, Lu GY, Quiocho FA;. J Biol Chem 1991;266:5202-5219.. [2]. 9360608. Structure of Haemophilus influenzae Fe(+3)-binding protein. reveals convergent evolution within a superfamily.. Bruns CM, Nowalk AJ, Arvai AS, McTigue MA, Vaughan KG, Mietzner. TA, McRee DE;. Nat Struct Biol 1997;4:919-924.. [3]. 9651355. Crystal structure and mutational analysis of the Escherichia. coli putrescine receptor. Structural basis for substrate. specificity.. Vassylyev DG, Tomitori H, Kashiwagi K, Morikawa K, Igarashi K;. J Biol Chem 1998;273:17604-17609.. [4]. 8336670. Structural, functional, and evolutionary relationships among. extracellular solute-binding receptors of bacteria.. Tam R, Saier MH Jr;. Microbiol Rev 1993;57:320-346. (from Pfam)
thiamine ABC transporter substrate-binding protein
The model describes thiamine ABC transporter, periplasmic protein in bacteria and archae. The protein belongs to the larger ABC transport system. It consists of at least three components: the thiamine binding periplasmic protein; an inner membrane permease; an ATP-binding subunit. It has been experimentally demonstrated that the mutants in the various steps in the de novo synthesis of the thiamine and the biologically active form, namely thiamine pyrophosphate can be exogenously supplemented with thiamine, thiamine monophosphate (TMP) or thiamine pyrophosphate (TPP).
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