1N8N

Crystal structure of the Au3+ complex of AphA class B acid phosphatase/phosphotransferase from E. coli at 1.69 A resolution

Summary for 1N8N

• Entry DOI: 10.2210/pdb1n8n/pdb
• Related: 1N9K
• Descriptor: Class B acid phosphatase, GOLD 3+ ION (3 entities in total)
• Functional Keywords: class b acid phosphatase, dddd acid phosphatase, metallo-enzyme, hydrolase
• Biological source: Escherichia coli
• Cellular location: Periplasm (Potential): P32697
• Total number of polymer chains: 1
• Total formula weight: 23752.31

Authors

Calderone, V.,Forleo, C.,Benvenuti, M.,Rossolini, G.M.,Thaller, M.C.,Mangani, S. (deposition date: 2002-11-21, release date: 2004-02-03, Last modification date: 2024-04-03)

Primary citation

Calderone, V.,Forleo, C.,Benvenuti, M.,Thaller, M.C.,Rossolini, G.M.,Mangani, S.
The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold.
J.Mol.Biol., 335:761-773, 2004

PubMed 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 2.2A and its resolution extended to 1.7A on an AuCl(3) 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.

PubMed: 14687572
DOI: 10.1016/j.jmb.2003.10.050

Experimental method

X-RAY DIFFRACTION (1.69 Å)