Crystallization of the maltodextrin-binding protein for active transport and chemotaxis in several different liganded and mutant forms.
We have crystallized the maltodextrin-binding protein complexed with two cyclic maltodextrins, and with no ligand at all. We have also grown crystals of two complexes of a mutant of maltodextrin-binding protein whose transport specificity has been altered. Studies of these crystals should provide considerable information about protein-oligosaccharide interactions, the effects of these interactions on oligosaccharide conformation, and particularly about the function of the periplasmic receptors in transport and chemotaxis.
Rodseth
L
L
Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77251.
Quiocho
F A
FA
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D001693:Biological Transport, Active; D002236:Carbohydrate Conformation; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D002633:Chemotaxis; D003460:Crystallization; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism*; D033902:Periplasmic Binding Proteins; D011485:Protein Binding; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C461619:MalE protein, E coli; D009844:Oligosaccharides; D033902:Periplasmic Binding Proteins; D011994:Recombinant Proteins