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An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases
1National Center for Biotechnology Information, National Institutes of Health, Bethesda, Maryland 20894, USA. neuwald@ncbi.nlm.nih.gov
Protein Science : a Publication of the Protein Society
|August 1, 1997
Abstract:
The mechanism of a membrane-bound enzyme important in phospholipid signaling, type 2 phosphatidic acid phosphatase, is suggested by sequence motifs shared with a soluble vanadium-dependent chloroperoxidase of known structure. These regions are also conserved in other soluble globular and membrane-associated proteins, including bacterial acid phosphatases, mammalian glucose-6-phosphatases, and the Drosophila developmental protein Wunen. This implies that a similar arrangement of catalytic residues specifies the active site within both soluble and membrane spanning domains.