Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases

0391455 - ÚMCH 2014 RIV GB eng J - Článek v odborném periodiku
Štěpánková, Andrea - Dušková, Jarmila - Skálová, Tereza - Hašek, Jindřich - Koval, Tomáš - Ostergaard, L. H. - Dohnálek, Jan
Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases.
Acta Crystallographica Section F-Structural Biology and Crystallization Communications. Roč. 69, č. 4 (2013), s. 346-354. ISSN 1744-3091. E-ISSN 2053-230X
Grant CEP: GA ČR GA310/09/1407; GA ČR GA305/07/1073; GA MŠMT EE2.3.30.0029
Výzkumný záměr: CEZ:AV0Z40500505
Institucionální podpora: RVO:61389013
Klíčová slova: organophosphorus acid anhydrolase * prolidases * bifunctional
Kód oboru RIV: CE - Biochemie
Impakt faktor: 0.568, rok: 2013

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, = 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 Ni2+ 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.
Trvalý link: http://hdl.handle.net/11104/0223536