The first structure of a bacterial class B acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold

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

Research output: Contribution to journalArticle

Abstract

AphA is a periplasmic acid phosphatase of Escherichia coli belonging to class B bacterial phosphatases, which is part of the DDDD superfamily of phosphohydrolases. The crystal structure of AphA has been determined at 2.2Å and its resolution extended to 1.7Å on an AuCl3 derivative. This represents the first crystal structure of a class B bacterial phosphatase. Despite the lack of sequence homology, the AphA structure reveals a haloacid dehalogenase-like fold. This finding suggests that this fold could be conserved among members of the DDDD superfamily of phosphohydrolases. The active enzyme is a homotetramer built by using an extended N-terminal arm intertwining the four monomers. The active site of the native enzyme, as prepared, hosts a magnesium ion, which can be replaced by other metal ions. The structure explains the non-specific behaviour of AphA towards substrates, while a structure-based alignment with other phosphatases provides clues about the catalytic mechanism.

Original languageEnglish
Pages (from-to)761-773
Number of pages13
JournalJournal of Molecular Biology
Volume335
Issue number3
DOIs
Publication statusPublished - Jan 16 2004

Keywords

  • Bacterial pathogens
  • Bacterial phosphatase
  • Class B phosphatase
  • Crystal structure
  • DDDD phosphatase superfamily
  • DESY, Deutsches Electronen Synchrotron
  • dNT-2, human mitochondrial 5′-3′ deoxyribonucleotidase

ASJC Scopus subject areas

  • Virology

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