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Protein Science, Vol 6, Issue 2 469-472, Copyright © 1997 by Cold Spring Harbor Laboratory Press
FOR THE RECORD |
J. STUKEY and G. M. CARMAN
Department of Biology, Hope College, Holland, Michigan 49422
We have identified a novel, conserved phosphatase sequence motif, KXXXXXXRP-(X(12-54))-PSGH-(X(31-54)-SRXXXXXHXXXD, that is shared among several lipid phosphatases, the mammalian glucose-6-phosphatases, and a collection of bacterial nonspecific acid phosphatases. This sequence was also found in the vanadium-containing chloroperoxidase of Curvularia inaequalis. Several lines of evidence support this phosphatase motif identification. Crystal structure data on chloroperoxidase revealed that all three domains are in close proximity and several of the conserved residues are involved in the binding of the cofactor, vanadate, a compound structurally similar to phosphate. Structure-function analysis of the human glucose-6-phosphatase has shown that two of the conserved residues (the first domain arginine and the central domain histidine) are essential for enzyme activity. This conserved sequence motif was used to identify nine additional putative phosphatases from sequence databases, one of which has been determined to be a lipid phosphatase in yeast.
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