3RVA
Crystal structure of organophosphorus acid anhydrolase from Alteromonas macleodii
Summary for 3RVA
| Entry DOI | 10.2210/pdb3rva/pdb |
| Descriptor | Organophosphorus acid anhydrolase, MANGANESE (II) ION, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | organophosphorus acid anhydrolase, pita-bread fold, binuclear metal center, bi-functional, prolidase, nerve agents, xaa-pro dipeptides, hydrolase |
| Biological source | Alteromonas macleodii |
| Total number of polymer chains | 1 |
| Total formula weight | 51786.32 |
| Authors | Stepankova, A.,Koval, T.,Ostergaard, L.H.,Duskova, J.,Skalova, T.,Hasek, J.,Dohnalek, J. (deposition date: 2011-05-06, release date: 2012-05-09, Last modification date: 2023-12-06) |
| Primary citation | Stepankova, A.,Duskova, J.,Skalova, T.,Hasek, J.,Koval, T.,Ostergaard, L.H.,Dohnalek, J. Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases. Acta Crystallogr.,Sect.F, 69:346-354, 2013 Cited by PubMed Abstract: 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 Å resolution in space group C2, with unit-cell parameters a = 133.8, b = 49.2, c = 97.3 Å, β = 125.0°. 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. PubMed: 23545636DOI: 10.1107/S1744309113002674 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
