A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases

Vito Calderone, Costantino Forleo, Manuela Benvenuti, Maria Cristina Thaller, Gian Maria Rossolini, Stefano Mangani

Research output: Contribution to journalArticle

Abstract

The Escherichia coli gene aphA codes for a periplasmic acid phosphatase called AphA, belonging to class B bacterial phosphatases, which is part of the DDDD superfamily of phosphohydrolases. After our first report about its crystal structure, we have started a series of crystallographic studies aimed at understanding of the catalytic mechanism of the enzyme. Here, we report three crystal structures of the AphA enzyme in complex with the hydrolysis products of nucleoside monophosphate substrates and a fourth with a proposed intermediate analogue that appears to be covalently bound to the enzyme. Comparison with the native enzyme structure and with the available X-ray structures of different phosphatases provides clues about the enzyme chemistry and allows us to propose a catalytic mechanism for AphA, and to discuss it with respect to the mechanism of other bacterial and human phosphatases.

Original languageEnglish
Pages (from-to)708-721
Number of pages14
JournalJournal of Molecular Biology
Volume355
Issue number4
DOIs
Publication statusPublished - Jan 27 2006

Keywords

  • Bacterial phosphatase
  • Catalytic mechanism
  • Class B phosphatase
  • Crystal structure
  • DDDD phosphohydrolase superfamily

ASJC Scopus subject areas

  • Virology

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