2g1a
Crystal structure of the complex between Apha class B acid phosphatase/phosphotransferase
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OverviewOverview
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.
About this StructureAbout this Structure
2G1A is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.
ReferenceReference
The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold., Calderone V, Forleo C, Benvenuti M, Cristina Thaller M, Maria Rossolini G, Mangani S, J Mol Biol. 2004 Jan 16;335(3):761-73. PMID:14687572
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