The crystal structure of a hyper-thermophilic carboxylesterase from the Archaeon Archaeoglobus fulgidus (Articolo in rivista)

Type
Label
  • The crystal structure of a hyper-thermophilic carboxylesterase from the Archaeon Archaeoglobus fulgidus (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1006/jmbi.2001.5152 (literal)
Alternative label
  • De Simone G., Menchise V., Manco G., Mandrich L., Sorrentino N., Lang D., Rossi M., Pedone C. (2001)
    The crystal structure of a hyper-thermophilic carboxylesterase from the Archaeon Archaeoglobus fulgidus
    in Journal of Molecular Biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Simone G., Menchise V., Manco G., Mandrich L., Sorrentino N., Lang D., Rossi M., Pedone C. (literal)
Pagina inizio
  • 507 (literal)
Pagina fine
  • 518 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • In questo lavoro è riportata la prima struttura cristallografica ad essere stata risolta per una esterasi ipertermofila, nel caso specifico AFEST da Archaeoglobus fulgidus. (literal)
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  • 314 (literal)
Rivista
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  • 12 (literal)
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  • Lavoro su rivista scientifica internazione in cui si riporta la caratterizzazione strutturale di una carbossiesterasi (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Centro di Studio di Biocristallografia- CNR University of Naples \"Federico II\", Naples, Italy Istituto di Biochimica delle Proteine ed Enzimologia-CNR, Naples, Italy EMBL c/o DESY, Hamburg, Germany (literal)
Titolo
  • The crystal structure of a hyper-thermophilic carboxylesterase from the Archaeon Archaeoglobus fulgidus (literal)
Abstract
  • The crystal structure of AFEST, a novel hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus, complexed with a sulphonyl derivative, has been determined and refined to 2.2 A resolution. This enzyme, which has recently been classified as a member of the hormone- sensitive-lipase (H) group of the esterase/lipase superfamily, presents a canonical alpha/beta hydrolase core, shielded on the C-terminal side by a cap region composed of five alpha-helices. It contains the catalytic triad Ser160, His285 and Asp255, whereby the nucleophile is covalently modified and the oxyanion hole formed by Gly88, Gly89 and Ala161. A structural comparison of AFEST with its mesophilic and thermophilic homologues, Brefeldin A esterase from Bacillus subtilis (BFAE) and EST2 from Alicyclobacillus acidocaldarius, reveals an increase in the number of intramolecular ion pairs and secondary structure content, as well as a significant reduction in loop extensions and ratio of hydrophobic to charged surface area. The variety of structural differences suggests possible strategies for thermostabilization of lipases and esterases with potential industrial applications. (literal)
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