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Structure of an aryl esterase from Pseudomonas fluorescens
KTH, Superseded Departments, Biochemistry and Biotechnology. Department of Chemistry, McGill University, Canada .
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2004 (English)In: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 60, no 7, 1237-1243 p.Article in journal (Refereed) Published
Abstract [en]

The structure of PFE, an aryl esterase from Pseudomonas fluorescens, has been solved to a resolution of 1.8 Å by X-ray diffraction and shows a characteristic α/β-hydrolase fold. In addition to catalyzing the hydrolysis of esters in vitro, PFE also shows low bromoperoxidase activity. PFE shows highest structural similarity, including the active-site environment, to a family of non-heme bacterial haloperoxidases, with an r.m.s. deviation in 271 Cα atoms between PFE and its five closest structural neighbors averaging 0.8 Å. PFE has far less similarity (r.m.s. deviation in 218 Cα atoms of 5.0 Å) to P. fluorescens carboxyl esterase. PFE favors activated esters with small acyl groups, such as phenyl acetate. The X-ray structure of PFE reveals a significantly occluded active site. In addition, several residues, including Trp28 and Met95, limit the size of the acyl-binding pocket, explaining its preference for small acyl groups.

Place, publisher, year, edition, pages
2004. Vol. 60, no 7, 1237-1243 p.
Keyword [en]
Pseudomonas fluorescens, arylesterase, carboxylesterase, threonine, article, binding site, chemical structure, chemistry, crystallization, enzymology, hydrolysis, metabolism, protein tertiary structure, stereoisomerism, X ray crystallography, Binding Sites, Carboxylic Ester Hydrolases, Crystallography, X-Ray, Models, Molecular, Protein Structure, Tertiary
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Biochemicals
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URN: urn:nbn:se:kth:diva-157769DOI: 10.1107/S0907444904010522ISI: 000222177600007Scopus ID: 2-s2.0-10044231181OAI: oai:DiVA.org:kth-157769DiVA: diva2:771780
Note

QC 20141215

Available from: 2014-12-15 Created: 2014-12-15 Last updated: 2017-12-05Bibliographically approved

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