Coordination and Stability of Calcium-Binding Site: D-Galactose/D-Glucose-Binding Protein of Bacterial Active Transport and Chemotaxis System

  • Nand K. Vyas
  • Meenakshi N. Vyas
  • Florante A. Quiocho


In the course of refining crystallographically the crystal structure of the D-galactose/ D-glucose-binding protein (Gal/GlcBP)1 at 1.9 Å resolution, we discovered a bound calcium (Vyas et al. 1987). The Gal/GlcBP is a member of a family of proteins (collectively called “binding proteins” which are located in the periplasmic space of Gram-negative bacteria. All binding proteins (~2 dozen) serve as initial receptors for the high-affinity active transport systems for a variety of amino acids, dipeptides, carbohydrates, and oxyanions (for recent reviews see Furlong 1987). Moreover, four of these proteins also act as receptors for bacterial chemotaxis (Macnab 1987). Each process further requires protein components lodged in the cytoplasmic membrane. The membrane components for active transport are the ones actually responsible in translocating nutrients from the periplasm to the cytoplasm. Translocation is triggered presumably by the interaction of the substrate-loaded binding proteins and each corresponding membrane component. On the other hand, the interaction between binding protein and transmembrane signal transducer proteins, the membrane components for chemotaxis, trigger taxis toward chemical attractants.


Peptide Unit Residue Loop Stereoscopic View Hydrogen Bond Array Octahedral Vertex 
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© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • Nand K. Vyas
  • Meenakshi N. Vyas
  • Florante A. Quiocho

There are no affiliations available

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