Structure of an aryl esterase from Pseudomonas fluorescens

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DOIResolve DOI: http://doi.org/10.1107/S0907444904010522
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TypeArticle
Journal titleActa Crystallographica Section D: Biological Crystallography
Volume60 Part 7
Pages12371243; # of pages: 7
SubjectHydrolysis; In Vitro; pha; x-ray
AbstractThe structure of PFE, an aryl esterase from Pseudomonas fluorescens, has been solved to a resolution of 1.8 Angstrom by X-ray diffraction and shows a characteristic alpha/beta-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 C-alpha atoms between PFE and its five closest structural neighbors averaging 0.8 Angstrom. PFE has far less similarity (r.m.s. deviation in 218 C-alpha atoms of 5.0 Angstrom) 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
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
NotePT: JournalIS: 0907-4449UD: 200431
Peer reviewedNo
NRC number46216
NPARC number3540271
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Record identifier1b142b1b-b264-4e50-8336-121150313b8e
Record created2009-03-01
Record modified2016-05-09
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