title: Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases.
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.
authors.affiliation: Institute of Macromolecular Chemistry, AS CR, vvi, Heyrovsky sq 2, 162 06 Prague 6, Czech Republic. a.stepanko@gmail.com
authors.forename: Andrea
authors.initials: A
authors.lastname: Štěpánková
authors.forename: Jarmila
authors.initials: J
authors.lastname: Dušková
authors.forename: Tereza
authors.initials: T
authors.lastname: Skálová
authors.forename: Jindřich
authors.initials: J
authors.lastname: Hašek
authors.forename: Tomáš
authors.initials: T
authors.lastname: Koval'
authors.forename: Lars H
authors.initials: LH
authors.lastname: Østergaard
authors.forename: Jan
authors.initials: J
authors.lastname: Dohnálek
mesh_terms: D020591:Alteromonas / Q000201:enzymology*; D000595:Amino Acid Sequence; D043303:Aryldialkylphosphatase / Q000737:chemistry*; D004150:Dipeptidases / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
chemical_list: D043303:Aryldialkylphosphatase; D004150:Dipeptidases; C022449:proline dipeptidase
keywords: bifunctional; organophosphorus acid anhydrolase; prolidases
references.citation: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):355-67
references.pmid: 21460454
references.citation: Arch Biochem Biophys. 2008 Jan 15;469(2):200-8
references.pmid: 17983589
references.citation: J Bacteriol. 1998 Sep;180(18):4781-9
references.pmid: 9733678
references.citation: J Ind Microbiol Biotechnol. 1997 Jan;18(1):49-55
references.pmid: 9079288
references.citation: J Mol Biol. 2007 Sep 21;372(3):774-97
references.pmid: 17681537
references.citation: Protein Sci. 2001 Feb;10(2):418-22
references.pmid: 11266627
references.citation: Arch Toxicol. 2004 Jun;78(6):338-43
references.pmid: 14985944
references.citation: Biochemistry. 2004 Mar 16;43(10):2771-83
references.pmid: 15005612
references.citation: Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):414-23
references.pmid: 15299395
references.citation: Biochim Biophys Acta. 2000 Mar 7;1477(1-2):157-67
references.pmid: 10708856
references.citation: Biophys J. 2000 Feb;78(2):719-30
references.pmid: 10653785
references.citation: Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):22-5
references.pmid: 20057045
references.citation: Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1744-54
references.pmid: 14501113
references.citation: J Synchrotron Radiat. 2012 May;19(Pt 3):442-9
references.pmid: 22514183
references.citation: Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):396-9
references.pmid: 12554964
references.citation: J Bacteriol. 1991 Mar;173(6):1938-43
references.pmid: 2001997
references.citation: Biochemistry. 2010 Jan 26;49(3):547-59
references.pmid: 20000741
references.citation: Protein Sci. 1995 Sep;4(9):1914-9
references.pmid: 8528088
references.citation: Nucleic Acids Res. 2000 Jan 1;28(1):235-42
references.pmid: 10592235
references.citation: Methods Enzymol. 1997;276:307-26
references.pmid: 27754618
references.citation: Bioinformatics. 1999 Apr;15(4):305-8
references.pmid: 10320398
references.citation: Biomacromolecules. 2005 May-Jun;6(3):1555-60
references.pmid: 15877378
references.citation: J Biol Chem. 1989 Mar 15;264(8):4476-81
references.pmid: 2925654
references.citation: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):386-94
references.pmid: 21460457
references.citation: Structure. 2001 Jun;9(6):493-502
references.pmid: 11435114
references.citation: Toxicol In Vitro. 2006 Feb;20(1):71-7
references.pmid: 16122899
references.citation: Arch Biochem Biophys. 2004 Sep 15;429(2):224-30
references.pmid: 15313226
references.citation: J Ind Microbiol Biotechnol. 2005 Dec;32(11-12):554-60
references.pmid: 16292554
references.citation: J Biol Chem. 1946 Jul;164:271-89
references.pmid: 20989488
references.citation: Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
references.pmid: 15572765
references.citation: Structure. 2001 Oct;9(10):987-97
references.pmid: 11591353
references.citation: Biochemistry. 1993 Apr 20;32(15):3907-12
references.pmid: 8471602
references.citation: Nucleic Acids Res. 1994 Nov 11;22(22):4673-80
references.pmid: 7984417
references.citation: Protein Sci. 2000 Jun;9(6):1063-72
references.pmid: 10892800