Crystallization and x-ray diffraction studies of a phosphate-binding protein involved in active transport in Escherichia coli.
We have obtained single crystals of a phosphate-binding protein (Mr = 34,400) that serves as initial receptor in osmotic shock-sensitive active transport in Escherichia coli. The crystals, suitable for high resolution crystallographic analysis, belong to the space group P2(1)2(1)2(1). The unit cell has dimensions of a = 41.97, b = 64.66, and c = 124.6 A and contains four protein molecules. Including this phosphate-binding protein, there are now a total of six different binding protein structures currently under investigation in our laboratory, the others being those specific for L-arabinose, D-galactose, D-maltose, sulfate, or leucine/isoleucine/valine.
D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D003460:Crystallization; D004926:Escherichia coli / Q000378:metabolism*; D028044:Phosphate-Binding Proteins; D010710:Phosphates / Q000378:metabolism; D011487:Protein Conformation; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D028044:Phosphate-Binding Proteins; D010710:Phosphates