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 2.2 Angstrom and its resolution extended to 1.7 Angstrom 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 nonspecific behaviour of AphA towards substrates, while a structure-based alignment with other phosphatases provides clues about the catalytic mechanism. (C) 2003 Elsevier Ltd. All rights reserved.

Calderone, V., Forleo, C., Benvenuti, M., Thaller, M.c., Rossolini, G., Mangani, S. (2004). The first structure of a bacterial class B acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold. JOURNAL OF MOLECULAR BIOLOGY, 335(3), 761-773 [10.1016/j.jmb.2003.10.050].

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

THALLER, MARIA CRISTINA;
2004-01-01

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 2.2 Angstrom and its resolution extended to 1.7 Angstrom 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 nonspecific behaviour of AphA towards substrates, while a structure-based alignment with other phosphatases provides clues about the catalytic mechanism. (C) 2003 Elsevier Ltd. All rights reserved.
2004
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/19 - MICROBIOLOGIA GENERALE
Settore CHIM/03 - CHIMICA GENERALE E INORGANICA
Settore MED/07 - MICROBIOLOGIA E MICROBIOLOGIA CLINICA
English
Con Impact Factor ISI
class B phosphatase; bacterial pathogens; bacterial phosphatase; DDDD phosphatase superfamily; crystal structure
Calderone, V., Forleo, C., Benvenuti, M., Thaller, M.c., Rossolini, G., Mangani, S. (2004). The first structure of a bacterial class B acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold. JOURNAL OF MOLECULAR BIOLOGY, 335(3), 761-773 [10.1016/j.jmb.2003.10.050].
Calderone, V; Forleo, C; Benvenuti, M; Thaller, Mc; Rossolini, G; Mangani, S
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/30859
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