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An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases
Author(s) -
Neuwald Andrew F.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060817
Subject(s) - phosphatase , biochemistry , phosphatidic acid , integral membrane protein , chemistry , active site , membrane , enzyme , membrane protein , acid phosphatase , peptide sequence , phospholipid , biology , gene
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.