1.3 angstrom structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family
Boltes I, Czapinska H, Kahnert A, Bulow von R, Dierks T, Schmidt B, Figura von K, Kertesz MA, Uson I (2001)
STRUCTURE 9(6): 483-491.
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Autor*in
Boltes, I;
Czapinska, H;
Kahnert, A;
Bulow von, R;
Dierks, ThomasUniBi;
Schmidt, B;
Figura von, K;
Kertesz, MA;
Uson, I
Einrichtung
Abstract / Bemerkung
Background: Sulfatases constitute a family of enzymes with a highly conserved active site region including a C alpha -formylglycine that is posttranslationally generated by the oxidation of a conserved cysteine or serine residue. The crystal structures of two human arylsulfatases, ASA and ASB, along with ASA mutants and their complexes led to different proposals for the catalytic mechanism in the hydrolysis of sulfate esters. Results: The crystal structure of a bacterial sulfatase from Pseudomonas aeruginosa (PAS) has been determined at 1.3 Angstrom. Fold and active site region are strikingly similar to those of the known human sulfatases. The structure allows a precise determination of the active site region, unequivocally showing the presence of a C alpha -formylglycine hydrate as the key catalytic residue. Furthermore, the cation located in the active site is unambiguously characterized as calcium by both its B value and the geometry of its coordination sphere. The active site contains a noncovalently bonded sulfate that occupies the same position as the one in para-nitrocate-cholsulfate in previously studied ASA complexes. Conclusions: The structure of PAS shows that the resting state of the key catalytic residue in sulfatases is a formylglycine hydrate. These structural data establish a mechanism for sulfate ester cleavage involving an aldehyde hydrate as the functional group that initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate. The alcohol is eliminated from a reaction intermediate containing pentacoordinated sulfur. Subsequent elimination of the sulfate regenerates the aldehyde, which is again hydrated. The metal cation involved in stabilizing the charge and anchoring the substrate during catalysis is established as calcium.
Erscheinungsjahr
2001
Zeitschriftentitel
STRUCTURE
Band
9
Ausgabe
6
Seite(n)
483-491
ISSN
0969-2126
Page URI
https://pub.uni-bielefeld.de/record/2350800
Zitieren
Boltes I, Czapinska H, Kahnert A, et al. 1.3 angstrom structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family. STRUCTURE. 2001;9(6):483-491.
Boltes, I., Czapinska, H., Kahnert, A., Bulow von, R., Dierks, T., Schmidt, B., Figura von, K., et al. (2001). 1.3 angstrom structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family. STRUCTURE, 9(6), 483-491. https://doi.org/10.1016/S0969-2126(01)00609-8
Boltes, I, Czapinska, H, Kahnert, A, Bulow von, R, Dierks, Thomas, Schmidt, B, Figura von, K, Kertesz, MA, and Uson, I. 2001. “1.3 angstrom structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family”. STRUCTURE 9 (6): 483-491.
Boltes, I., Czapinska, H., Kahnert, A., Bulow von, R., Dierks, T., Schmidt, B., Figura von, K., Kertesz, M. A., and Uson, I. (2001). 1.3 angstrom structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family. STRUCTURE 9, 483-491.
Boltes, I., et al., 2001. 1.3 angstrom structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family. STRUCTURE, 9(6), p 483-491.
I. Boltes, et al., “1.3 angstrom structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family”, STRUCTURE, vol. 9, 2001, pp. 483-491.
Boltes, I., Czapinska, H., Kahnert, A., Bulow von, R., Dierks, T., Schmidt, B., Figura von, K., Kertesz, M.A., Uson, I.: 1.3 angstrom structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family. STRUCTURE. 9, 483-491 (2001).
Boltes, I, Czapinska, H, Kahnert, A, Bulow von, R, Dierks, Thomas, Schmidt, B, Figura von, K, Kertesz, MA, and Uson, I. “1.3 angstrom structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family”. STRUCTURE 9.6 (2001): 483-491.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
INTERPRO
1 Eintrag gefunden, die diesen Artikel zitieren
PDB
1 Eintrag gefunden, die diesen Artikel zitieren
x-ray diffraction (PDB: 1hdh)
Protein structure name: arylsulfatase from pseudomonas aeruginosa
Public wwPDB file in PDB format
Protein structure name: arylsulfatase from pseudomonas aeruginosa
Public wwPDB file in PDB format
UNIPROT
1 Eintrag gefunden, die diesen Artikel zitieren
Arylsulfatase (UNIPROT: P51691)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Download in FASTA format
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Download in FASTA format
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