2B82

Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with adenosine and phosphate bound to the catalytic metal at 1.2 A resolution

Replaces:  1RMW

Summary for 2B82

• Entry DOI: 10.2210/pdb2b82/pdb
• Related: 1N8N 1N9K 2B8J
• Descriptor: class B acid phosphatase, MAGNESIUM ION, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: class b acid phosphatase; dddd acid phosphatase; metallo-enzyme; amp, hydrolase
• Biological source: Escherichia coli
• Cellular location: Periplasm (Potential): P32697
• Total number of polymer chains: 2
• Total formula weight: 47709.56

Authors

Calderone, V.,Forleo, C.,Benvenuti, M.,Thaller, M.C.,Rossolini, G.M.,Mangani, S. (deposition date: 2005-10-06, release date: 2005-11-29, Last modification date: 2023-08-23)

Primary citation

Calderone, V.,Forleo, C.,Benvenuti, M.,Thaller, M.C.,Rossolini, G.M.,Mangani, S.
A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases
J.Mol.Biol., 355:708-721, 2006

PubMed 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.

PubMed: 16330049
DOI: 10.1016/j.jmb.2005.10.068

Experimental method

X-RAY DIFFRACTION (1.25 Å)