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Metallophosphoesterases: structural fidelity with functional promiscuity

Matange, Nishad and Podobnik, Marjetka and Visweswariah, Sandhya S (2015) Metallophosphoesterases: structural fidelity with functional promiscuity. In: BIOCHEMICAL JOURNAL, 467 (2). pp. 201-216.

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Official URL: http://dx.doi.org/10.1042/BJ20150028

Abstract

Calcineurin-like metallophosphoesterases (MPEs) form a large superfamily of binuclear metal-ion-centre-containing enzymes that hydrolyse phosphomono-, phosphodi-or phosphotri-esters in a metal-dependent manner. The MPE domain is found in Mre11/SbcD DNA-repair enzymes, mammalian phosphoprotein phosphatases, acid sphingomyelinases, purple acid phosphatases, nucleotidases and bacterial cyclic nucleotide phosphodiesterases. Despite this functional diversity, MPEs show a remarkably similar structural fold and active-site architecture. In the present review, we summarize the available structural, biochemical and functional information on these proteins. We also describe how diversification and specialization of the core MPE fold in various MPEs is achieved by amino acid substitution in their active sites, metal ions and regulatory effects of accessory domains. Finally, we discuss emerging roles of these proteins as non-catalytic protein-interaction scaffolds. Thus we view the MPE superfamily as a set of proteins with a highly conserved structural core that allows embellishment to result in dramatic and niche-specific diversification of function.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the PORTLAND PRESS LTD, CHARLES DARWIN HOUSE, 12 ROGER STREET, LONDON WC1N 2JU, ENGLAND
Keywords: GpdQ; metalloenzyme; metallophosphoesterase; Mre11; phosphoester; Rv0805
Department/Centre: Division of Biological Sciences > Molecular Reproduction, Development & Genetics
Depositing User: Id for Latest eprints
Date Deposited: 06 May 2015 04:50
Last Modified: 06 May 2015 04:50
URI: http://eprints.iisc.ac.in/id/eprint/51477

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