PMID:9385653

Citation	Sigrell, JA, Cameron, AD, Jones, TA and Mowbray, SL (1997) Purification, characterization, and crystallization of Escherichia coli ribokinase. Protein Sci. 6:2474-6
Abstract	Ribokinase phosphorylates ribose to form ribose-5-phosphate in the presence of ATP and magnesium. The phosphorylated sugar can enter the pentose phosphate pathway or be used for the synthesis of nucleotides, histidine, and tryptophan. Ribokinase belongs to the PfkB family of carbohydrate kinases, for which no three-dimensional structure is currently known. We describe an improved purification protocol for Escherichia coli ribokinase and give evidence from light-scattering and gel filtration studies that the protein forms a dimer in solution. Several types of crystals are also described that have been obtained of apo ribokinase, ribokinase in the presence of ATP, and in a ternary complex with an ATP-analogue and ribose. The latter crystals give the best X-ray diffraction. A complete data set has been collected at the synchrotron source in Hamburg, to 2.6 A resolution using a frozen crystal. The crystals belong to space group P6(1)22 or P6(5)22 with cell parameters a = b = 95 A and c = 155 A.
Links	PubMed PMC2143589 Online version:10.1002/pro.5560061124
Keywords	Crystallography, X-Ray; Dimerization; Escherichia coli/enzymology; Phosphotransferases (Alcohol Group Acceptor)/chemistry
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