2B82: Crystal Structure Of Apha Class B Acid PhosphatasePHOSPHOTRANSFERASE Ternary Complex With Adenosine And Phosphate Bound To The Catalytic Metal At 1.2 A Resolution

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.
PDB ID: 2B82Download
MMDB ID: 36168
PDB Deposition Date: 2005/10/6
Updated in MMDB: 2005/12
Experimental Method:
x-ray diffraction
Resolution: 1.25  Å
Source Organism:
Similar Structures:
Biological Unit for 2B82: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 2B82
Label Count Molecule
Proteins (4 molecules)
Class B Acid Phosphatase
Molecule annotation
Chemicals (12 molecules)
* Click molecule labels to explore molecular sequence information.

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