3RVA: Crystal structure of organophosphorus acid anhydrolase from Alteromonas macleodii

The bacterial enzyme organophosphorus acid anhydrolase (OPAA) is able to catalyze the hydrolysis of both proline dipeptides (Xaa-Pro) and several types of organophosphate (OP) compounds. The full three-dimensional structure of the manganese-dependent OPAA enzyme is presented for the first time. This enzyme, which was originally isolated from the marine bacterium Alteromonas macleodii, was prepared recombinantly in Escherichia coli. The crystal structure was determined at 1.8 A resolution in space group C2, with unit-cell parameters a = 133.8, b = 49.2, c = 97.3 A, beta = 125.0 degrees . The enzyme forms dimers and their existence in solution was confirmed by dynamic light scattering and size-exclusion chromatography. The enzyme shares the pita-bread fold of its C-terminal domain with related prolidases. The binuclear manganese centre is located in the active site within the pita-bread domain. Moreover, an Ni(2+) ion from purification was localized according to anomalous signal. This study presents the full structure of this enzyme with complete surroundings of the active site and provides a critical analysis of its relationship to prolidases.
PDB ID: 3RVADownload
MMDB ID: 99337
PDB Deposition Date: 2011/5/6
Updated in MMDB: 2012/05
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3RVA: dimeric; determined by author and by software (PISA)
Molecular Components in 3RVA
Label Count Molecule
Proteins (2 molecules)
Organophosphorus Acid Anhydrolase
Molecule annotation
Chemicals (8 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB