Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5455
Title: Structural Insights into the Catalytic Mechanism of the Bacterial Class B Phosphatase AphA Belonging to the DDDD Superfamily of Phosphohydrolases
Authors: R., Leone
E., Cappelletti
Benvenuti, Manuela 
G., Lentini
M. C., Thaller
Mangani, Stefano 
Keywords: x-ray; crystal structure; phosphatase; magnesium; mechanism
Issue Date: 2008
Project: None 
Journal: JOURNAL OF MOLECULAR BIOLOGY
Abstract: 
AphA is a magnesium-dependent, bacterial class B acid phosphatase that catalyzes the hydrolysis of a variety of phosphoester substrates and belongs to the DDDD superfamily of phosphohydrolases. The recently reported crystal structure of AphA from Escherichia coli has revealed the quaternary structure of the enzyme together with hints about its catalytic mechanism. The present work reports the crystal structures of AphA from E. coli in complex with substrate, transition-state, and intermediate analogues. The structures provide new insights into the mechanism of the enzyme and allow a revision of some aspects of the previously proposed mechanism that have broader implications for all the phosphatases of the DDDD superfamily. (C) 2008 Elsevier Ltd. All rights reserved.
Description: 
47920
URI: http://hdl.handle.net/20.500.12779/5455
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2008.09.050
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