Davies, Lyndsay and Anderson, Ian P. and Turner, Philip C. and Shirras, Alan D. and Rees, Huw H. and Rigden, Daniel J. (2007) An unsuspected ecdysteroid/steroid phosphatase activity in the key T-cell regulator, Sts-1: Surprising relationship to insect ecdysteroid phosphate phosphatase. Proteins: Structure, Function, and Bioinformatics, 67 (3). pp. 720-731.Full text not available from this repository.
The insect enzyme ecdysteroid phosphate phosphatase (EPP) mobilizes active ecdysteroids from an inactive phosphorylated pool. Previously assigned to a novel class, it is shown here that it resides in the large histidine phosphatase superfamily related to cofactor-dependent phosphoglycerate mutase, a superfamily housing notably diverse catalytic activities. Molecular modeling reveals a plausible substrate-binding mode for EPP. Analysis of genomic and transcript data for a number of insect species shows that EPP may exist in both the single domain form previously characterized and in a longer, multidomain form. This latter form bears a quite unexpected relationship in sequence and domain architecture to vertebrate proteins, including Sts-1, characterized as a key regulator of T-cell activity. Long form Drosophila melanogaster EPP, human Sts-1, and a related protein from Caenorhabditis elegans have all been cloned, assayed, and shown to catalyse the hydrolysis of ecdysteroid and steroid phosphates. The surprising relationship described and explored here between EPP and Sts-1 has implications for our understanding of the function(s) of both.
|Journal or Publication Title:||Proteins: Structure, Function, and Bioinformatics|
|Uncontrolled Keywords:||insect hormone • histidine phosphatase superfamily • ecdysone phosphate phosphatase • molecular modeling • evolutionary relationship|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited By:||Dr Alan Shirras|
|Deposited On:||09 Jun 2008 09:19|
|Last Modified:||07 Jan 2015 16:16|
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