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Structure of an aryl esterase from Pseudomonas fluorescens
KTH, Tidigare Institutioner, Biokemi och biokemisk teknologi. Department of Chemistry, McGill University, Canada .
Vise andre og tillknytning
2004 (engelsk)Inngår i: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 60, nr 7, s. 1237-1243Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2004. Vol. 60, nr 7, s. 1237-1243
Emneord [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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Identifikatorer
URN: urn:nbn:se:kth:diva-157769DOI: 10.1107/S0907444904010522ISI: 000222177600007Scopus ID: 2-s2.0-10044231181OAI: oai:DiVA.org:kth-157769DiVA, id: diva2:771780
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QC 20141215

Tilgjengelig fra: 2014-12-15 Laget: 2014-12-15 Sist oppdatert: 2017-12-05bibliografisk kontrollert

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