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Titolo:
The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus
Autore:
De Simone, G; Menchise, V; Manco, G; Mandrich, L; Sorrentino, N; Lang, D; Rossi, M; Pedone, C;
Indirizzi:
Univ Naples Federico II, Ctr Studio Biocristallog, CNR, I-80134 Naples, Italy Univ Naples Federico II Naples Italy I-80134 CNR, I-80134 Naples, Italy CNR, Inst Biochim Prot & Enzimol, I-80125 Naples, Italy CNR Naples ItalyI-80125 t Biochim Prot & Enzimol, I-80125 Naples, Italy DESY, European Mol Biol Lab, D-22603 Hamburg, Germany DESY Hamburg Germany D-22603 pean Mol Biol Lab, D-22603 Hamburg, Germany
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 3, volume: 314, anno: 2001,
pagine: 507 - 518
SICI:
0022-2836(20011130)314:3<507:TCSOAH>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
HORMONE-SENSITIVE LIPASE; ALPHA/BETA-HYDROLASE FOLD; PYROCOCCUS-FURIOSUS; SEQUENCE SIMILARITY; SALT BRIDGES; HYPERTHERMOPHILIC PROTEINS; ELECTROSTATIC INTERACTIONS; GLUTAMATE-DEHYDROGENASE; BACILLUS-ACIDOCALDARIUS; THERMOSTABLE ESTERASE;
Keywords:
crystal structure; esterase; hyper-thermophilic enzyme; alpha/beta hydrolase fold; lipase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
68
Recensione:
Indirizzi per estratti:
Indirizzo: Pedone, C Univ Naples Federico II, Ctr Studio Biocristallog, CNR, Via Mezzocannone 6-8, I-80134 Naples, Italy Univ Naples Federico II Via Mezzocannone 6-8 Naples Italy I-80134
Citazione:
G. De Simone et al., "The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus", J MOL BIOL, 314(3), 2001, pp. 507-518

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 Angstrom 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 Ala16l. A structural comparison of AFEST with its mesophilic and thermophilic homologues, Brefeldin A esterasefrom 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. (C) 2001 AcademicPress.

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Documento generato il 14/07/20 alle ore 05:25:28