Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5201
Title: A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases
Authors: V., Calderone
C., Forleo
Benvenuti, Manuela 
M. C., Thaller
Rossolini, GIAN MARIA
Mangani, Stefano 
Keywords: x-ray; crystal structure; phosphatase; magnesium; mechanism
Issue Date: 2006
Project: None 
Journal: JOURNAL OF MOLECULAR BIOLOGY
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. (c) 2005 Elsevier Ltd. All rights reserved.
Description: 
47929
URI: http://hdl.handle.net/20.500.12779/5201
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2005.10.068
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