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

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Description	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. 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. (en)
Title	Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases (en)
skos:prefLabel	Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases (en)
skos:notation	RIV/61389013:_____/13:00391455!RIV14-MSM-61389013
http://linked.open...avai/predkladatel	Ústav makromolekulární chemie AV ČR, v. v. i.
http://linked.open...avai/riv/aktivita	I P Z
http://linked.open...avai/riv/aktivity	I, P(EE2.3.30.0029), P(GA305/07/1073), P(GA310/09/1407), Z(AV0Z40500505)
http://linked.open...iv/cisloPeriodika	4
http://linked.open...vai/riv/dodaniDat	2014
http://linked.open...aciTvurceVysledku	Kovaľ, Tomáš Štěpánková, Andrea Dohnálek, Jan Hašek, Jindřich Skálová, Tereza Dušková, Jarmila
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Ústav makromolekulární chemie AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	94626
http://linked.open...ai/riv/idVysledku	RIV/61389013:_____/13:00391455
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	organophosphorus acid anhydrolase; prolidases; bifunctional (en)
http://linked.open.../riv/klicoveSlovo	bifunctional organophosphorus acid anhydrolase prolidases
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[EF434CE0706D]
http://linked.open...i/riv/nazevZdroje	Acta Crystallographica Section F
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	6 (xsd:int)
http://linked.open...cetTvurcuVysledku	7 (xsd:int)
http://linked.open...vavai/riv/projekt	Chitinolytic enzymes from Clostridium paraputrificum inhabiting the human gastrointestinal tract; structure and biomedical implications. Molecular interactions of polymers for biomedical applications BIOPOL: BIOpolymer POstdoc Laboratory and educative center
http://linked.open...UplatneniVysledku	2013
http://linked.open...v/svazekPeriodika	69
http://linked.open...iv/tvurceVysledku	Dohnálek, Jan Dušková, Jarmila Hašek, Jindřich Skálová, Tereza Štěpánková, Andrea Ostergaard, L. H. Koval, Tomáš
http://linked.open...ain/vavai/riv/wos	000316949100002
http://linked.open...n/vavai/riv/zamer	Progresivní makromolekulární materiály a supramolekulární systémy: syntéza a studium vlastností, jevů a možností využití pro speciální aplikace a moderní technologie
issn	1744-3091
number of pages	9 (xsd:int)
http://bibframe.org/vocab/doi	10.1107/S1744309113002674

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